mumps introduction for assignment

Learn how UpToDate can help you.

Select the option that best describes you

• Medical Professional
• Resident, Fellow, or Student
• Hospital or Institution
• Group Practice
• Patient or Caregiver
• Find in topic

RELATED TOPICS

INTRODUCTION

The epidemiology, clinical manifestations, diagnosis, treatment, and prevention of mumps are discussed here. Issues related to vaccination for prevention of mumps are discussed separately. (See "Measles, mumps, and rubella immunization in infants, children, and adolescents" and "Measles, mumps, and rubella immunization in adults" .)

EPIDEMIOLOGY

Before the United States mumps vaccination program began in 1967, about 186,000 cases were reported each year; the actual number of cases was likely much higher due to underreporting. Since implementation of routine vaccination, there has been a more than 99 percent decrease in mumps cases in the United States [ 2 ]. (See "Measles, mumps, and rubella immunization in infants, children, and adolescents" and "Measles, mumps, and rubella immunization in adults" .)

From year to year in the United States, mumps cases can range from a few hundred to a few thousand ( figure 1 ) [ 3-5 ]. The number of cases reported in 2016 and 2017 (6369 and 5629, respectively) were the highest in a decade [ 6 ].

On this page

When to see a doctor, complications.

Mumps is an illness caused by a virus. It usually affects the glands on each side of the face. These glands, called parotid glands, make saliva. Swollen glands may be tender or painful.

Salivary glands

There are three pairs of major salivary glands — parotid, sublingual and submandibular. Each gland has its own tube (duct) leading from the gland to the mouth.

Mumps are not common in the United States because of vaccines. But outbreaks do happen. People who are not vaccinated are at high risk of infection. Vaccinated people who get mumps usually have milder symptoms and fewer complications.

There is no specific medicine for mumps. Treatment relieves pain and discomfort.

Symptoms of mumps show up about 2 to 3 weeks after exposure to the virus. Some people may have no symptoms or very mild symptoms.

The first symptoms may be similar to flu symptoms such as:

• Muscle aches or pain.
• Not wanting to eat.

Swelling of the salivary glands usually starts within a few days. Symptoms may include:

• Swelling of one or both glands on the sides of the face.
• Pain or tenderness around the swelling.
• Less often, swelling of glands below the floor of the mouth.

A common symptom of mumps is painful swelling on one or both sides of the face.

See your health care provider if you or your child has symptoms of mumps. Mumps spreads very easily for about five days after the swelling starts. If you think you have mumps, let the clinic know before you go. The clinic staff likely will take steps to prevent the spread of disease.

Other conditions may have similar symptoms, so it's important to get a quick diagnosis.

If you think your child has mumps, call your care provider if your child develops:

• Fever of 103 F (39 C) or greater.
• Trouble eating or drinking.
• Confusion or disorientation.
• Stomach pain.
• Pain and swelling of the testicles.

In the meantime:

• Rest as much as possible.
• Use pain relievers you can get without a prescription, such as ibuprofen (Advil, Motrin IB, others) and acetaminophen (Tylenol, others).
• Use a cold or warm cloth over swollen salivary glands.

From Mayo Clinic to your inbox

Mumps is caused by a type of germ called a virus. When someone has mumps, the virus is in saliva. Coughing or sneezing can release tiny droplets with the virus into the air.

You can get the virus by breathing in tiny droplets. Or you can get the virus by touching a surface where droplets have landed and then touching your face. You also can pick up the virus from direct contact, such as kissing or sharing a water bottle.

Outbreaks in the United States most often happen where people live or work in close contact. These may include college campuses, summer camps and schools.

Complications of mumps are more likely among people who aren't vaccinated. They can happen even if a person didn't have swollen salivary glands.

Complications happen when the virus reaches other tissues in the body. Complications may include:

• Swollen testicles. This complication, also called orchitis, causes severe pain. It's more common with a mumps infection after puberty. A swollen testicle may lead to a decrease in the size of the testicle and a decline in fertility.
• Swollen ovaries. This complication, also caused oophoritis, causes pain, upset stomach, vomiting and fever. This complication is more likely after puberty. The condition doesn't seem to affect fertility.
• Encephalitis . Encephalitis is swelling, called inflammation, in the brain that may damage tissues. This complication can cause changes in consciousness, seizures and loss of muscle control.
• Meningitis. Meningitis is swelling, or inflammation, of the membranes around the brain and spinal cord. It may cause head, fever and neck stiffness. Meningitis related to mumps rarely causes long-term problems.
• Hearing loss. This complication can happen suddenly or over time. Hearing usually gets better after the illness.
• Pancreatitis. Mumps can cause damage to the pancreas, called pancreatitis, from swelling. Symptoms may include pain or tenderness near the stomach, upset stomach, vomiting and fever.
• Miscarriage. Getting mumps during the first 12 weeks of pregnancy may increase the risk that a pregnancy will end, called miscarriage.

History of mumps: Outbreaks and vaccine timeline

Most people who have had the mumps vaccines, called fully vaccinated, are protected from mumps infections. People who aren't vaccinated are more likely to get mumps.

For some people, vaccine protection may go down over time. When fully vaccinated people get mumps, they usually have milder symptoms and fewer complications.

The MMR vaccine

The mumps vaccine is a part of the recommended childhood vaccinations. It's usually given as a combined measles-mumps-rubella (MMR) vaccine. The schedule is:

• The first dose between the ages of 12 and 15 months.
• The second dose between the ages of 4 and 6 years before entering school.

Another version of measles-mumps-rubella (MMR) includes the vaccine against the virus that causes chickenpox, called varicella-zoster virus. But that vaccine, called the measles-mumps-rubella-varicella vaccine (MMRV) is not used for the first dose in the standard vaccination schedule for children.

Extensive studies in several countries have shown that there is no link between the MMR or measles-mumps-rubella-varicella (MMRV) vaccines and autism. The original study that suggested this connection in 1998 was based on scientific errors. That study was removed from the scientific record in 2010.

Extensive reports from the American Academy of Pediatrics, the National Academy of Medicine, and the Centers for Disease Control and Prevention conclude that there is no scientifically proven link between the MMR vaccine and autism.

People who need the MMR vaccine

If you haven't had two doses or aren't sure, talk to your health care provider. You may need two doses of the vaccine or a booster. This is especially important if you are in a high-risk setting or in an outbreak. The following people may need proof of vaccination or more doses:

• College students.
• People in the military.
• International travelers.
• Health care workers.

People who don't need the MMR vaccine

If you're not sure if you're vaccinated, a blood test can show whether you have antibodies to mumps. If you have antibodies to the virus, then your immune system would fight a mumps infection and you don't need another vaccine.

People who were born before 1957 were likely exposed to the virus. They likely are immune to mumps.

The mumps vaccine is made from a weak but still infectious mumps virus. A typical immune system can handle this weak virus easily. But people with immune systems that won't respond quickly or strongly to the vaccine don't usually get this vaccine. But there are some exceptions if the benefits outweigh the risks. Also, this type of vaccine is not suggested for people who are pregnant.

Side effects of the MMR vaccine

The MMR vaccine is safe and effective. Most people have no side effects.

If they happen, mild side effects may include:

• Soreness at the site of the shot.
• Rash at the site of the shot.
• Swelling of the glands in the cheeks or neck.

In rare cases, some people may have symptoms such as pain and stiffness in joints, seizures, short-term drop in blood platelets or a rash.

Severe allergic reactions are rare. People who have a severe allergic reaction to the first dose aren't given a second dose. Also, people won't get the vaccine if they've had a severe allergic reaction to an ingredient in the vaccine.

Nov 23, 2022

• AskMayoExpert. Mumps. Mayo Clinic; 2022.
• Mumps: For health care providers. U.S. Centers for Disease Control and Prevention. https://www.cdc.gov/mumps/hcp.html. Accessed Oct. 24, 2022.
• Albrect MA. Mumps. https://www.uptodate.com/contents/search. Accessed Oct. 24, 2022.
• Bennett JE, et al. Mumps virus. In: Mandell, Douglas, and Bennett's Principles and Practice of Infectious Diseases. 9th ed. Elsevier; 2020. https://www.clinicalkey.com. Accessed Oct. 24, 2022.
• Kliegman RM, et al. Mumps. In: Nelson Textbook of Pediatrics. 21st ed. Elsevier; 2020. https://www.clinicalkey.com. Accessed Oct. 24, 2022.
• AskMayoExpert. Measles-mumps-rubella (MMR) vaccination. Mayo Clinic; 2022.
• Immunization: Mumps. U.S. Department of Health and Human Services. https://www.hhs.gov/immunization/diseases/mumps/index.html. Accessed Oct. 26, 2022.
• CDC studies on vaccines and autism. U.S. Centers for Disease Control and Prevention. https://www.cdc.gov/vaccinesafety/concerns/thimerosal/index.html. Accessed Oct. 24, 2022.
• Understanding thimerosal, mercury, and vaccine safety. U.S. Centers for Disease Control and Prevention. https://www.cdc.gov/vaccinesafety/concerns/thimerosal/index.html. Accessed Oct. 24, 2022.
• Thimerosal and vaccines. U.S. Centers for Disease Control and Prevention. https://www.cdc.gov/vaccinesafety/concerns/thimerosal/index.html. Accessed Oct. 24, 2022.
• Vaccine safety for moms-to-be. U.S. Centers for Disease Control and Prevention. https://www.cdc.gov/vaccines/pregnancy/vacc-safety.html. Accessed Oct. 31, 2022.
• The editors of the Lancet. Retraction: Ileal-lymphoid-nodular hyperplasia, non-specific colitis, and pervasive developmental disorder in children. The Lancet. 2010. doi: 10.1016/S0140-6736(10)60175-4
• Autism and Vaccines. Centers for Disease Control and Prevention. https://www.cdc.gov/vaccinesafety/concerns/autism.html. Accessed Nov. 15, 2022.
• Diseases & Conditions
• Mumps symptoms & causes

More Information

CON-XXXXXXXX

Your gift holds great power – donate today!

Make your tax-deductible gift and be a part of the cutting-edge research and care that's changing medicine.

Mumps Programming Language Textbook

• Mumps Language Tutorial (PDF)
• Mumps Open Source Code Distribution
• Some Example Mumps Programs
• Input Titles and Abstracts for YouTube Examples
• MumpsBookCode.tar.gz
• YouTube Mumps Programming Language Tutorial & Examples

The MUMPS Programming Language

Cite this chapter.

• B. I. Blum &
• H. F. Orthner  

Part of the book series: Computers and Medicine ((C+M))

139 Accesses

1 Citations

A programming language is a specialized language—with a syntax (a grammar) and semantics (the meanings of correct statements)—that can be processed by a computer. In effect, the programming language is the interface between the designer of a system and the computer that implements it. Because there are many different types of systems, there are also many different types of programming languages.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

• Available as PDF
• Read on any device
• Instant download
• Own it forever
• Available as EPUB and PDF
• Compact, lightweight edition
• Dispatched in 3 to 5 business days
• Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Unable to display preview.  Download preview PDF.

Bibliographic Note

COBOL: D.D. McCracken, A Simplified Guide to Structured COBOL Programming, John Wiley, New York, 1976. ( McCracken has a clear, mature style and his books for any language are to be recommended. )

Google Scholar  

FORTRAN: J. W. Crowley and C. E. Miller, A Structured Approach to FORTRAN, Prentice Hall, 1983; Chirlian, P., Introduction to Structured Fortran, Matrix Publishers, 1979; and A. Balfour, D. H. Marwick, Programming in Standard FORTRAN 77, North Holland, Amsterdam, 1982.

ALGOL: D. Brailsford and A. Walker, Introductory Algol-68 Programming, Wiley, New York, 1979.

PL/ 1: J. Hughes, PL/ I Structured Programming, 2nd ed, Wiley, New York, 1979.

PASCAL: R. Conway, I). Gries, E. C. Zimmerman, A Primer on Pascal, Little, Brown, 1981, and P Gregono, Programming in PASCAL, Addison Wesley, Reading, MA 1980.

BASIC: There are a large number of introductory texts. Most systems come with one.

FORTH: H. Katzen, Invitation to FORTH, Petrocelli, 1981.

APL: R. P Polivka and S. Pakin, APL The Language and Its Usage, Prentice-Hall, New York 1975.

Ada: P Wegner, Programming with Ada, Prentice-Hall, New York 1980.

LISP: P H. Winston, LISP, AddisonWesley, 1981.

PROLOG: W. F. Clocksin and C. S. Mellish, Programming in PROLOG, Springer Verlag, New York, 1981.

Arthur F. Krieg, David H. Miller, and Gregory L. Bressler, Computer Programming in Standard MUMPS ( second edition ), MUMPS Users’ Group, College Park, MD, 1984.

Thomas C. Salander, Introduction to Standard MUMPS: A Guide for the Novice, MUMPS Users’ Group, College Park, MD, 1984.

Charles S. Volkstorf, The MUMPS Handbook of Efficiency Techniques: 125 Ways to Make Your MUMPS Application Run Faster, MUMPS Users’ Group, College Park, MD, 1985.

Richard F. Walters, Jack Bombe, and J.C. Wilcox, MUMPS Primer: An Introduction to the Interactive Programming System of the Future, MUMPS Users’ Group, College Park, MD, 1983.

Thomas C. Salander and Hairlan Stenn, ANS MUMPS: Programmers’ Reference Manual 1985, MUMPS Users’ Group, College Park, MD, 1985.

David B. Brown and Donald H. Glaeser, A Cookbook of MUMPS: Programmer’s Tech-niques and Routines, Comp. Computing, Inc., Houston, TX, 1985 (available from the MUMPS Users’ Group, College Park, MD).

Stephan Hesse and Wolfgang Kirsten, Einfuhrung in die Programmiersprache MUMPS, Walter de Gruyter, Berlin, New York, 1983 (in German).

John Lewkowicz, The Complete MUMPS, Prentice Hall, Englewood Cliffs, NJ, 1988.

Ruth E. Dayhoff (ed.), MUG Quarterly, MUMPS Users’ Group, College Park, MD (this is a periodical which also includes the proceedings of the annual MUG meetings).

Download references

You can also search for this author in PubMed   Google Scholar

Editor information

Editors and affiliations.

Academic Computer Services, George Washington University Medical Center, 20037, Washington, D.C., USA

Helmuth F. Orthner Ph.D. ( Director ) ( Director )

Applied Physics Laboratory, Johns Hopkins University, 20707, Laurel, Maryland, USA

Bruce I. Blum ( Principal Professional Staff ) ( Principal Professional Staff )

Rights and permissions

Reprints and permissions

Copyright information

© 1989 Springer-Verlag New York Inc.

About this chapter

Blum, B.I., Orthner, H.F. (1989). The MUMPS Programming Language. In: Orthner, H.F., Blum, B.I. (eds) Implementing Health Care Information Systems. Computers and Medicine. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-3488-3_23

Download citation

DOI : https://doi.org/10.1007/978-1-4612-3488-3_23

Publisher Name : Springer, New York, NY

Print ISBN : 978-1-4612-8122-1

Online ISBN : 978-1-4612-3488-3

eBook Packages : Springer Book Archive

Share this chapter

Anyone you share the following link with will be able to read this content:

Sorry, a shareable link is not currently available for this article.

Provided by the Springer Nature SharedIt content-sharing initiative

• Publish with us

Policies and ethics

• Find a journal
• Track your research

An official website of the United States government

The .gov means it’s official. Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

The site is secure. The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

• Publications
• Account settings

Preview improvements coming to the PMC website in October 2024. Learn More or Try it out now .

• Advanced Search
• Journal List

Exploring the Mumps Virus Glycoproteins: A Review

Jasmine rae frost.

1 Department of Medical Microbiology and Infectious Diseases, Faculty of Health Sciences, University of Manitoba, Winnipeg, MB R3T 2N2, Canada; ac.abotinamuym@3tsorfmu (J.R.F.); ac.abotinamuym@shkiahs (S.S.)

Saba Shaikh

Alberto severini.

2 JC Wilt Infectious Diseases Research Centre, NMLB, Public Health Agency of Canada, Winnipeg, MB R3E 3R2, Canada

Associated Data

Not applicable.

The resurgence of mumps in vaccinated adult populations has raised concerns about possible waning vaccine immunity or a potential lack of protection to the circulating strain. A number of individual studies have investigated if there are amino acid variations between the circulating wild-type strains and vaccine strains. In these studies, the HN and F mumps surface glycoproteins have been of interest, because of their role in viral infection, and because the HN protein is the target of neutralizing antibodies. Here, we summarize the single nucleotide variants and their potential effect that have been identified between mumps genotypes in the HN and F proteins.

1. Introduction

Mumps has seen a re-emergence in recent years, even in highly vaccinated populations. The more recent outbreaks have shown a change in demographic: mumps is no longer a disease of young children, but instead, cases are occurring mainly in young adults [ 1 , 2 , 3 , 4 , 5 ]. What is driving this re-emergence is unknown, but it is likely due to waning vaccine immunity or a lack of cross-reactivity between the circulating strains and the vaccine strain [ 6 , 7 , 8 , 9 ].

There are 12 mumps genotypes (A–N), determined by sequencing of the more diverse mumps region, the small hydrophobic (SH) gene [ 10 ]. Currently, only six genotypes are circulating world-wide (C, D, F, G, H, and K) [ 11 ]. Mumps genotype G accounts for over 50% of genotyped cases world-wide, including those in the outbreaks that have been seen in Canada, USA, the Netherlands and other European countries [ 12 , 13 , 14 , 15 , 16 ]. In Canada and the USA, the mumps component of the MMR vaccine belongs to the Jeryl Lynn strain, which is a mixture of two (JL2 and JL5) closely related genotype A viruses [ 17 ]. As the vaccine is a different genotype than the current circulating strain, it is possible that antibodies produced through vaccination are not fully effective against this genotype [ 6 , 18 ]. Current evidence suggests there may be a difference in the ability to neutralize the circulating genotype G compared to the vaccine genotype A. In one study, prior to infection with mumps, individuals had lower antibody titers to a genotype G virus than genotype A [ 6 ]. Similarly, it has been shown that there are variances in patient serum in the ability to neutralize a genotype G virus when compared to the vaccine strain [ 19 ]. These studies suggest a lack of cross-reactivity, which may be a contributing factor in the more recent mumps outbreaks. Interestingly, there have also been epitope differences identified between the vaccine strain and the circulating strain [ 8 , 13 , 18 , 20 ]. These differences could explain the apparent lack of protection from the vaccine.

A similar trend has also been observed in China, where the S79 vaccine (a derivative of the Jeryl Lynn strain) is used. Here, the major circulating strains are of genotype F, but similarly to the outbreaks observed elsewhere with genotype G, differences in neutralization between the vaccine and circulating strain have been observed [ 21 ]. One difference between the outbreaks in China and those seen elsewhere is that China currently only has a single MMR dose recommendation in their vaccination plan, which studies have shown is not sufficient to provide full protection. This has allowed mump incidence rates to remain high [ 21 ].

The mumps RNA genome is 15,384 nucleotides in length and encodes seven genes: the nucleoprotein (N), the Phosphoproteins (P/V), the matrix protein (M), the fusion protein (F), the small hydrophobic protein (SH), the hemagglutinin-neuraminidase protein (HN) and the large protein (L) [ 5 , 22 ]. The genomic organization of mumps is 3′ N-P-M-F-SH-HN-L 5′, which are on tandemly linked transcription units [ 22 , 23 ]. The two surface glycoproteins of the mumps virus are the HN and F proteins. These glycoproteins are essential for viral entry to host cells, and the spread of newly formed virions [ 24 , 25 , 26 ].

In addition to being critical for viral entry, the HN protein has been shown to be the target of neutralizing antibodies [ 27 ]. These factors, and the fact that a number of B- and T-cell epitope differences have been identified between vaccine strains and circulating strains of mumps, have made these glycoproteins an area of interest in the search to identify what is driving the re-emergence of mumps [ 13 , 20 , 28 , 29 ]. The goal of this review is to summarize differences that have been identified in the HN and F mumps proteins.

2. Search Strategy

A literature search was performed using the key words: Mumps, MuV, AND Jeryl Lynn, Genotype A, MuVA, Genotype G, MuVG, AND/OR HN, Epitope, Antigenicity, F, Fusion Protein, Hemagglutinin protein, Surface protein, Matrix protein, M protein, Neutral*. The search results are summarized in Table 1 . The literature search was performed in September 2020, to OVID MEDLINE ® Embase and Scopus. A second search was performed in January 2022 to include more recent literature. Additional articles were selected from the citations of articles from the primary search.

Search terms and results for the literature search of mumps epitopes.

Note: * Represents the truncation symbol used in the databases.

3. The Hemagglutinin-Neuraminidase Protein

The hemagglutinin-neuraminidase (HN) protein is a 582-amino acid structural glycoprotein of the mumps virus [ 30 ]. HN is a type II membrane protein in which the N terminus is oriented towards the cytoplasm and the C terminus is extracellular [ 31 ]. The HN crystal structure has been determined for the genotype B Hoshino strain (Protein Data Bank entry 5B2D and 5B2C) [ 26 ]. This structure confirmed that like other paramyxoviruses, the mumps HN head domain shows a six-bladed β-propeller fold (β1−β6 sheets) and forms a homodimer. Two homodimers form a tetramer, again similar to other paramyxoviruses [ 26 , 31 ]. This protein contains a number of conserved motifs: a leucine zipper, the neuraminidase motif and the hemagglutinin receptor binding site (GAEGRV) [ 32 , 33 ].

The HN protein exhibits both hemagglutinin and neuraminidase properties and is critical for membrane fusion and viral entry into host cells [ 34 ]. The HN protein binds preferentially to trisaccharides with α-2,3 linked sialic acid in unbranched sugars ( Figure 1 ). Binding to the glycan motifs sialyl Lewis x (SLe x ) and GM2 ganglioside (GM2-glycan) has also been identified [ 35 ]. Various sialyated glycan structures can be found in tissues and organs throughout the body, which may explain both the viral tropism for glandular tissues and the spread of mumps throughout the body [ 26 ]. The neuraminidase properties of this protein are due to the conserved linear sequence NRKSCS. This sequence is found throughout the paramyxovirus family [ 32 ]. The HN protein cleaves sialic acid residues from progeny viruses, preventing agglutination and allowing for viral release from the host cell [ 26 , 36 ]. In coordination with the F protein, the HN protein will mediate both cell to cell fusion and virus to cell fusion allowing for the spread of viral particles to other host cells [ 5 ]. The helix-bundled stalk of the HN protein is thought to play a critical role in the activation of the F protein. The dimer–dimer interactions found in the tetrameric head domain of the HN protein seem to be important in the role of the HN protein triggering the F protein for fusion [ 37 , 38 ].

Protein structures generated from Protein Data Base file 5B2D [ 26 ]. ( A ) Protein binding sites and N-glycosylation sites of mumps HN protein (front view). Illustrated are the HN protein (purple), N-acetyl-D-glucosamine binding sites (pink), and sialic acid receptor binding sites (green). Different N-glycosylation sites are labelled with arrows and boxes indicate the amino acid range. ( B ) Protein binding sites and N-glycosylation sites of mumps HN protein (back view). Illustrated are the HN protein (purple), N-acetyl-D-glucosamine binding sites (pink), and sialic acid receptor binding sites (green). Different N-glycosylation sites are labelled with arrows and boxes indicate the amino acid range.

4. HN Protein Structure

The HN protein is a major target of immune response in mumps infection [ 28 ]. It is also a major target of the anti-mumps antibodies produced by vaccination [ 39 ]. It has been shown that there are antigenic differences between HN proteins of different mumps genotypes. In particular, genotype A seems to be antigenically distinct from genotypes B, C and D [ 40 , 41 , 42 , 43 ]. A study using monoclonal antibodies raised against the HN protein of a genotype A virus (SBL-1) compared the B-cell epitopes of genotypes A, C, D, G and H viruses and identified different reactivity profiles between the genotype A viruses compared to other genotypes. Additionally, different genotypes have been compared in neutralization tests using rabbit hyper immune sera against genotypes A or D. Here, there was not a clear difference in neutralization patterns between the genotypes C, D, G, H and I. However, genotype A was serologically distinct, showing high neutralization titers against Kilham strain and much lower neutralization titers against SBL-1 or RW (genotype D) strains [ 40 , 43 ].

The mumps HN protein has nine N-linked glycosylation sites at amino acids 12–14, 127–129, 284–286, 329–331, 400–402, 448–450, 464–466, 507–509 and 514–516 ( Figure 1 ) [ 41 , 44 ]. Mutations in sites 12–14 and 127–129, found in genotype G strains, and site 464–466, in vaccine strains (JL5 and JL2), result in loss of N-glycosylation [ 39 , 45 ]. The sites 127–129 and 464–466 can have a cysteine as the variable residues, while site 514–516 can have a proline, which would affect the glycosylation of these sites [ 41 ]. The residues 35–53 (ILVLSVQAVILILVIVTLG) are a membrane anchorage site [ 46 ]. In a study of the L-Zagreb vaccine strain, it was found that position 51 was an asparagine, not a threonine, while other strains showed this region to be conserved [ 47 ]. The effect of this change is unclear.

The regions 265–288, 329–340, and 352–360 on the HN protein have been found to be antigenic ( Figure 2 ) [ 40 , 47 , 48 ]. When these regions are mapped, they can be seen on the surface of the HN protein, and therefore would be able to interact with antibodies [ 49 ]. Within these regions, there are observed amino acid differences between strains ( Table 2 ) [ 46 ]. The region between amino acids 329–340 has been used to immunize mice. Antibodies from this immunization were shown to be able to induce neutralizing antibodies against wild-type mumps strains, and thus they could contain a critical epitope for humoral immune response [ 48 ]. Single nucleotide variants (SNVs) between genotypes that occur in significant areas of the HN protein have been looked at with interest, as changes in this immune-dominant protein could help explain the re-emergence of mumps that has been seen in vaccinated populations.

Currently known HN amino acid variants in wild-type viruses when compared to vaccine strains.

Note: * indicates variant was not conserved in all samples in the study.

Protein structures generated from Protein Data Base file 5B2D [ 26 ]. ( A ) Protein binding sites and known epitopes of mumps HN protein (Front view). Protein binding sites and N-glycosylation sites of Mumps HN Protein (back view). Illustrated are the HN protein (purple), N-acetyl-D-glucosamine binding sites (pink), and sialic acid receptor binding sites (green). Different epitope locations are labelled with arrows and boxes indicate the amino acid range. ( B ) Protein binding sites and known epitopes of mumps HN protein (back view). Protein binding sites and N-glycosylation sites of mumps HN Protein (back view). Illustrated are the HN protein (purple), N-acetyl-D-glucosamine binding sites (pink), and sialic acid receptor binding sites (green). Different epitope locations are labelled with arrows and boxes indicate the amino acid range.

5. HN B-Cell and T-Cell Epitopes

A number of B- and T-cell epitopes have been identified for the HN protein, either through computational analysis or through in vitro assays. The following regions have been predicted to be B-cell epitopes: 199–207, 220–240 261–266, 269–272, 284–296, 327–331 and 334–363. The regions 261–266 and 269–272 have been experimentally validated to be neutralizing epitopes. This was determined by the production of virus escape mutants, which were then tested for antibody recognition via ELISA using antibodies that had been shown to bind specific regions of the HN protein [ 40 , 47 , 49 ]. Five T-cell recognition regions have been predicted (74–82, 88–96, 157–165, 326–334, 503–513) of which amino acid variations in four of the regions (74–82, 157–165, 326–334, 503–513) have been shown to reduce HLA binding for genotype G [ 50 ]. When the predicted mumps epitopes on the HN protein are mapped, they are predicted to fall near α- helices in the HN head domain. These α- helices show diversity between different genotypes, which may play a role in the outbreaks of mumps that are occurring in vaccinated individuals [ 26 ].

The regions 113–130, 375–403 and 440–443 have been identified as potential regions involved in evading neutralization [ 42 ]. They have also been described as potential epitopes, and are thought to have a dominant role compared to other epitope sites [ 42 ].

A mumps outbreak in Arkansas USA allowed for the opportunity to compare a large number of genotype G strains against the Jeryl Lynn vaccine strain. When B-cell epitopes were predicted for the HN protein, there were clear differences between the circulating genotype G strains and genotype A. A total of 28 amino acid positions were predicted to be in B-cell epitopes on the HN gene. From these, 5 were unique to genotype G strains only (8, 25, 26, 166, and 167), while 17 positions were unique to the vaccine strains, JL5 and JL2 (58, 59, 232, 300, 425, 438, 439, 448, 449, 450, 451, 452, 453, 487, 488, 497, and 532) [ 13 ].

6. Other HN SNVs

Neuro-virulence had been previously associated with the amino acids 335, 354, 356, 360, 464, and 466 [ 47 , 51 , 52 , 53 , 54 ]. However, conflicting studies have shown that identical mumps sequences can be isolated from patients both with and without neurological symptoms [ 44 ]. It seems unlikely these residues alone are responsible for causing the neurological symptoms that are seen in some cases of mumps infection. The actual cause of this is still unknown.

A number of studies have investigated genomic differences between the locally used vaccine strain and the currently circulating local strains. As genotype G strains account for over 50% of cases genotyped world-wide, many studies focus on the differences between this and the Jeryl Lynn vaccine genotype A strain [ 11 ].

In the JL5 component of the Jeryl Lynn vaccine, the amino acid 279 is an isoleucine, but in wild-type viruses, it is a threonine. Similarly, position 287 in JL5 is an isoleucine, but in wild-type viruses, it is a valine. These changes have been predicted to result in differences in T-cell and B-cell epitopes, which results in a mismatch of CD4+ and CD8+ responses in an exposure to wild-type viruses [ 42 ]. A large study comparing mainly B- and T-cell epitopes of North American sequences (genotype G) to the major component of the MMR vaccine, JL5, found four consistent amino acid changes, which included the positions 279 and 287. The amino acid changes I279T, and I287V have been predicted to be vaccine escape mutations. These changes in amino acids are hypothesized to result in a loss of a T-helper epitope, preventing the induction of B-cell stimulation [ 29 ]. The Arkansas study identified SNVs at amino acid positions: I279T, I287V, L336S, and E356D. When the potential structural changes were investigated, they observed that large amino acids were replaced with smaller ones which did result in structural changes [ 55 ]. They also hypothesize that the changes L336S and I287V may affect HN protein and antibody binding as these are located in known B- and T-cell epitopes. In particular, the L336S SNV is predicted to strengthen the HN protein as it allows for the formation of added hydrogen bonds with amino acids [ 55 ]. Amino acid variations of JL5 compared to other mumps genotypes showed mutations at positions: K74M, R76K, E77A, A80T, A158A/F, H161R, V334I/L, T511A and T513A/I, resulting in reduce HLA binding which could affect T-cell Immunogenicity [ 50 ].

A study from the Netherlands comparing circulating genotype G sequences against the vaccine genotype A strain identified eight positions that contained differences, which were located in five known B-cell epitope regions. The amino acid variants found in positions A37V, G63S, H94Y, T97M, T129S, A153S, K317R and S330G were genotype G specific. A number of other variable sites were identified, although not all of them were conserved between all sequences ( Table 2 ) [ 8 ].

Additionally, a SNV (N464K) in the HN protein in the Jeryl Lynn vaccine strains JL5 and JL2 can cause a loss in glycosylation. SNVs at position N12S and T129S in genotype G strains have resulted in loss of N-glycosylation. This sites are bordered by neutralizing epitopes [ 39 , 47 ].

Similar to the genotype G outbreaks of mumps seen worldwide, China has experience mumps outbreaks, but of a circulating genotype F virus [ 56 ]. In a study of genotype F mumps viruses circulating in China, it was determined that the HN amino acid variants L6F, D25N, V81M, V218A, V249I, T288I, A406S, and T474A increased in frequency in wild-type genotype F sequences from 2001–2015. From this study, it was found that 30 HN SNVs occurred in at least 50% of wild-type samples studied [ 21 ]. A second study of strains circulating in China identified the SNV A474V [ 56 ].

In a study of HN sequences of mumps viruses found to be circulating in Korea from 1998–2016, (genotypes F, H and I) against the Jeryl Lynn vaccine strain, the authors found no changes in protein glycosylation sites. They did identify the following amino acid variants between the vaccine genotypes and circulating strains: I279T, I287V, L336S, and E356D, in known neutralizing epitope sites. They also identified SNVs in new predicted epitopes/ vaccine escapes sites: N121S, R122K, N123K/E and Y442S [ 7 ].

In comparative studies of the Jeryl Lynn vaccine strain against geographic specific circulating strains, the positions 279, 287, 336, and 356 appear often. Table 2 lists all variable sites that have been identified to date [ 57 ]. Further investigations are needed to determine if or how these SNVs are playing a role in the mumps outbreaks occurring in young adult populations.

7. The Fusion Protein

The mumps fusion protein (F) is a 538-amino acid, class one fusion surface glycoprotein [ 60 ]. It is responsible for the membrane fusion of virus and host cell [ 61 ]. The un-cleaved protein has three hydrophobic regions: an amino-terminal signal peptide, an amino terminal region of F1 and the carboxyl-terminal membrane domain [ 62 ]. This protein starts as a precursor molecule (F0), and is then cleaved into the active protein by the recognition of a R-X-L/R-R motif by a host endoprotease (furin) [ 63 ]. The F protein contains two disulfide-linked polypeptides (F1 and F2) [ 61 ]. The fusion core from the mumps Miyahara strain (genotype B) has been crystalized (protein data base entry 2FYZ) [ 61 ]. The structure of the mumps F protein is similar to other paramyxovirus. This glycoprotein has two discontinuous heptad repeat domains at the ectodomain [ 61 , 64 ]. The core complex forms a six-helix bundle, and forms a 3-4-4-4-3 spacing that has also been seen in other viruses such as RSV [ 61 ].

The role of the fusion glycoprotein is to mediate the fusion of lipid membranes, and this occurs at a neutral pH. Binding of the HN protein to a receptor signals the F protein to undergo the conformational change needed to drive the fusion of the viral and cell membranes [ 24 , 25 ].

8. F Protein Structure

In the mumps fusion protein, the first 19 amino acids act as a signal peptide to promote the F protein function [ 62 , 65 ]. This sequence has been shown to vary between strains, unlike the region 98–102, which is recognized by the cell proteases and is strongly conserved [ 46 ]. Residues 483–512 (IGAIICAALCLSILSIIISLLFCCWAYIAT) comprise a membrane anchorage [ 62 ]. In the L-Zagreb strain position 489 contains a threonine not an alanine [ 46 ].

The amino acid 195 is known to play an important role in the fusogenicity of the virus [ 66 ]. In the L-Zagreb and Urabe strains, there is a phenylalanine in this position, while the Jeryl Lynn components, Rubini, Hoshino, and Miyahara strains, have a serine [ 46 ].

The fusion protein also contains glycosylation sites at positions: 73–75, 182–184, 352–354, 427–429, 433–435, 457–459 [ 62 ].

9. F Protein Epitopes

A number of B-cell epitopes have been identified for the mumps F protein. In a study using anti-mumps mAbs, the amino acid positions 221, 323, and 373 were determined to be located in at least two conformational neutralization epitopes. Glycosylation at position 373, or the loss of glycosylation at position 323 in genotype G strains, resulted in a mechanism of escape from the mAbs [ 67 ]. Using prediction software to model the F protein, it has been determined that residues 221 and 373 are distant and must be on separate epitopes in the monomeric form. However, in a homotrimer model, these residues can be found in a closer proximity to each other [ 67 ].

A comparison between genotype G sequences from a mumps outbreak in Arkansas and the components of the MMR vaccine (JL5 and JL2) found distinct predicted B-cell epitope amino acid positions on the F protein. From the 17 total predicted positions, genotype G predicted B-cell positions were found at amino acid positions: 19, 88, 159, 173, 174, 353, 368, 435, 461 and 515. Positions 173 and 368 were unique to the wild-type genotype G viruses. The vaccine strains also had unique predicted epitope positions at amino acid positions 18, 27, 324, 344, 350, and 412 [ 13 ]. These areas will be of interest in future studies, as structural differences in B- and T-cell epitopes could lead to a change in immune system recognition.

10. F Protein SNVs

Similar to the mumps HN protein, many studies have explored differences in the Jeryl Lynn vaccine strain to the circulating strain, often genotype G ( Table 3 ). Differences between genotype A mumps and genotypes D, C and B have been noted at amino acid positions T7I, I13V, V49I, S318R, S345T, A409S and N480S. Some genotype C and D samples showed alternate variants at positions S318G and A409T [ 65 ]. Interestingly the variants in amino acids T7I and I13V occur in the signal peptide of the N terminus. Similar to what has been observed with the HN protein, it was determined that the mumps A genotype was not as closely related as the B, C and D genotypes [ 65 ]. A study comparing circulating genotype G strains against the genotype A Jeryl Lynn vaccine strain in the Netherlands identified the mutation S97L as a SNV of interest. As this variant is found near the cleavage site that results in the conformational change in the F protein, the authors hypothesized it may play a role in enhancing the fusion process because of the increase in hydrophobicity [ 8 ].

List of known F protein amino acid variants and their properties.

Note: * indicates the mutation was not conserved between samples in the study.

Other variants of note include the strain RS-12, which has an isoleucine at position 269, instead of the methionine found in circulating sequences [ 59 ]. Additionally, a study of circulating genotype F strains in China found the following SNVs: V151I and H329Y [ 56 ]. How these amino acid variants are affecting immune responses in individuals is not yet clear.

11. Discussion

The re-emergence of mumps is a trend that has been seen worldwide, and is occur-ring in vaccinated young adult populations [ 4 , 15 , 16 , 68 , 69 , 70 ]. These outbreaks are caused by a mumps genotype that differs from the vaccine genotype used in that region. Most outbreaks are due to a mumps genotype G, while the vaccine that is used in the same area is the Jeryl Lynn strain, which is a mixture of two genotype A strains (JL5 and JL2) [ 11 , 12 , 16 , 71 ]. The factors that are driving these outbreaks are unclear, but there is evidence to suggest a difference in cross-reactivity or a difference in the viral epitopes may be playing a role [ 6 , 19 ].

Differences in neutralization between vaccine strains and circulating strains have been observed in many studies [ 8 , 42 , 72 , 73 ]. The reason for these differences is not well understood, but one popular hypothesis is it could be due to the differences in the functional or immunological properties of the mumps HN and F glycoproteins. A number of difference have been identified in the mumps HN and F glycoproteins. A large study conducted in the USA found 32 amino acid site substitutions between their circulating stains and the Jeryl Lynn HN protein (the component of the vaccine used in the USA). The majority of the amino acid variations were conserved between the outbreak sequences and a previously sequenced strain that had been shown to have a lower degree of neutralization than the Jeryl Lynn strain [ 8 , 19 , 70 ].

12. Conclusions

While it is still unclear if the changes in the mumps glycoproteins are the cause of recent outbreaks, the number of differences observed between vaccine and circulating strains suggests this could be a factor. Future studies will need to be carried out to determine how the changes in glycoproteins effect antibody recognition. Screening for future variants will also be important in subsequent outbreaks. This review summarized what is known to date on the mumps HN and F glycoproteins and their epitopes.

Funding Statement

This research received no external funding.

Author Contributions

Conceptualization, J.R.F. and S.S.; methodology, J.R.F. and S.S.; writing—original draft preparation, J.R.F. and S.S.; writing—review and editing, A.S., J.R.F. and S.S.; supervision, A.S. All authors have read and agreed to the published version of the manuscript.

Institutional Review Board Statement

Informed consent statement, data availability statement, conflicts of interest.

The authors declare no conflict of interest.

Publisher’s Note: MDPI stays neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Official websites use .gov

A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS

A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

For Healthcare Providers

Clinical features, transmission, complications, mumps during pregnancy, mumps in vaccinated people, vaccination, case classification, laboratory tests to diagnose mumps, reporting mumps cases.

• Prevention and Control in Healthcare Settings

From the Merck Manual Consumer Version, edited by Robert Porter. Copyright 2015 by Merck Sharp & Dohme Corp., a subsidiary of Merck & Co, Inc, Kenilworth, NJ. Available at merckmanuals.com . Accessed June 2015.

Mumps is a viral illness caused by a paramyxovirus, a member of the Rubulavirus family. The average incubation period for mumps is 16 to 18 days, with a range of 12 to 25 days.

NEW: Recommendations for Measles, Mumps, Rubella and Varicella Testing for Clinicians [9 pages]

To learn more about how to promptly recognize and diagnose mumps, check out this Mumps Clinical Diagnosis Fact Sheet [2 pages] .

Mumps usually involves pain, tenderness, and swelling in one or both parotid salivary glands (cheek and jaw area). Swelling usually peaks in 1 to 3 days and then subsides during the next week. The swollen tissue pushes the angle of the ear up and out. As swelling worsens, the angle of the jawbone below the ear is no longer visible. Often, the jawbone cannot be felt because of swelling of the parotid. One parotid may swell before the other, and in 25% of patients, only one side swells. Other salivary glands (submandibular and sublingual) under the floor of the mouth also may swell but do so less frequently (10%).

Nonspecific prodromal symptoms may precede parotitis by several days, including low-grade fever which may last 3 to 4 days, myalgia, anorexia, malaise, and headache. Parotitis usually lasts on average 5 days and most cases resolve after 10 days. Mumps infection may also present only with nonspecific or primarily respiratory symptoms, or may be asymptomatic. Reinfection after natural infection and recurrent parotitis, when parotitis on one side resolves but is followed weeks to months later by parotitis on the other side, can also occur in mumps patients.

Mumps can occur in a person who is fully vaccinated, but vaccinated patients are less likely to present severe symptoms or complications than under- or unvaccinated cases. Mumps should be suspected in all patients with parotitis or mumps complications, regardless of age, vaccination status, and travel history.

Mumps infection is most often confused with swelling of the lymph nodes of the neck. Lymph node swelling can be differentiated by the well-defined borders of the lymph nodes, their location behind the angle of the jawbone, and lack of the ear protrusion or obscuring of the angle of the jaw, which are characteristics of mumps.

While not a common symptom of flu, swelling of their salivary glands (parotitis) has been reported in persons with laboratory-confirmed influenza infections. To learn more, see 2016-2017 Influenza Update for Health Care Providers: Parotitis and Influenza .

Before the U.S. mumps vaccination program started in 1967, about 186,000 cases were reported each year, and many more unreported cases occurred. The disease caused complications, such as permanent deafness in children, and occasionally, encephalitis, which could rarely result in death. Following the implementation of the routine two dose MMR vaccination policy, there was a 99% decrease in mumps cases in the United States, with just a few hundred cases reported each year by the early 2000s. However, starting in 2006 there has been an increase in mumps cases with several peak years. From year to year, the number of mumps cases can range from roughly a couple hundred to a several thousand, with majority of cases and outbreaks occurring among people who are fully vaccinated and in close-contact or congregate settings.

The mumps virus replicates in the upper respiratory tract and is transmitted person to person through direct contact with saliva or respiratory droplets of a person infected with mumps. The risk of spreading the virus increases the longer and the closer the contact a person has with someone who has mumps. The infectious period is considered from 2 days before to 5 days after parotitis onset, although virus has been isolated from saliva as early as 7 days prior to and up to 9 days after parotitis onset. Mumps virus has also been isolated up to 14 days in urine and semen.

When a person is ill with mumps, they should avoid contact with others from the time of diagnosis until 5 days after the onset of parotitis by staying home from work or school and staying in a separate room if possible.

Mumps complications include orchitis, oophoritis, mastitis, meningitis, encephalitis, pancreatitis, and hearing loss. Complications can occur in the absence of parotitis and occur less frequently in vaccinated patients. Some complications of mumps are known to occur more frequently among adults than children.

Orchitis occurs in approximately 30% of unvaccinated and 6% of vaccinated post-pubertal male mumps patients. In 60% to 83% of males with mumps orchitis, only one testis is affected. Mumps orchitis has not been linked to infertility, but may result in testicular atrophy and hypofertility. Among adolescent and adult female mumps patients in the United States in the post-vaccine era, rates of oophoritis and mastitis have been ≤1%. However, these complications may be more difficult to recognize and are likely underreported. Pancreatitis, deafness, meningitis, and encephalitis have been reported in less than 1% of cases in recent U.S. outbreaks. Cases of nephritis and myocarditis and other sequelae, including paralysis, seizures, cranial nerve palsies, and hydrocephalus, in mumps patients have been reported but are very rare. Death from mumps is exceedingly rare. There have been no mumps-related deaths reported in the United States during recent mumps outbreaks.

Mumps that occurs in pregnant women is generally benign and not more severe than in women who are not pregnant. Like other infections, there is a theoretical risk that mumps during the early months of pregnancy may cause complications. Most studies on the effects of gestational mumps on the fetus were conducted in the 1950s–60s when the disease was more common before mumps vaccine was available. One study from 1966 reported an association between mumps infection during the first trimester of pregnancy and an increase in the rate of spontaneous abortion or intrauterine fetal death 1 , but this result has not been observed in other studies 2 . One study of low birth weight in relation to mumps during pregnancy found no significant association 1 . While there are case reports of congenital malformations in infants born to mothers who had mumps during pregnancy, the only prospective, controlled study found rates of malformations were similar between mothers who had mumps and those who did not have mumps during pregnancy 3 .

Learn more about preventing infections during pregnancy .

People who previously had one or two doses of MMR vaccine can still get mumps and transmit the disease. During mumps outbreaks in highly vaccinated communities, the proportion of cases that occur among people who have been vaccinated may be high. This does not mean that the vaccine is ineffective. The effectiveness of the vaccine is assessed by comparing the attack rate in people who are vaccinated with the attack rate in those who have not been vaccinated. In outbreaks of highly vaccinated populations, people who have not been vaccinated against mumps usually have a much greater mumps attack rate than those who have been fully vaccinated. Disease symptoms are generally milder and complications are less frequent in vaccinated people.

Vaccination is the best way to prevent mumps and mumps complications. This vaccine is included in the combination measles-mumps-rubella (MMR) and measles-mumps-rubella-varicella (MMRV) vaccines. Two doses of mumps vaccine are 88% (range 32% to 95%) effective at preventing the disease; one dose is 78% (range 49% to 91%) effective.

In October 2017, the Advisory Committee on Immunization Practices (ACIP) recommended that people identified by public health authorities as being part of a group at increased risk for acquiring mumps because of a mumps outbreak should receive a third dose of MMR vaccine. The purpose of the recommendation is to improve protection of people in outbreak settings against mumps disease and mumps-related complications.

• Your health department will provide information on groups at increased risk who should receive a dose. If you suspect an outbreak, or are unsure if your patient belongs to a group at increased risk, contact your local health department for more information.
• You should not give a third dose unless your patient is part of a group at increased risk as determined by your local public health authorities.
• MMR vaccine has not been shown to prevent illness in persons already infected with mumps and should not be used as post-exposure prophylaxis in immediate close contacts. However, close contacts should still be offered a dose to help protect them against future exposures in the event their prior exposures did not result in infection.

See Mumps Vaccination  for vaccination recommendations.

For information about how to classify mumps cases, visit the Laboratory Testing Section of the Manual for the Surveillance of Vaccine-Preventable Diseases (2018), Chapter 9: Mumps .

RT-PCR and viral culture are used to confirm mumps infection. Buccal swabs are most commonly used for RT-PCR testing, but urine and CSF may also be used in specific situations . IgM serology can also be used to aid in diagnosing mumps infection. A patient’s vaccination status and timing of specimen collection are important for interpreting laboratory results. A negative test result does not rule out mumps infection.

Mumps is a nationally notifiable disease, and all cases should be reported to the state or local health department. Contact your state health department  for more information on how to report mumps in your state.

Mumps Prevention and Control in Healthcare Settings

Mumps transmission in healthcare settings, while not common, has occurred in past outbreaks, involving hospitals and long-term care facilities housing adolescents and adults. Information about what measures to take to prevent and control mumps in healthcare settings can be found under the Healthcare Setting section of the Manual for the Surveillance of Vaccine-Preventable Diseases (2018), Chapter 9: Mumps

• Siegel M, Fuerst HT, Peress NS. Comparative fetal mortality in maternal virus diseases. A prospective study on rubella, measles, mumps, chicken pox and hepatitis. N Engl J Med 1966;274(14):768-71.
• Wilson CB, Nizet V, Maldonado YA, Remington JS, Klein JO. Remington and Klein’s infectious diseases of the fetus and newborn infant . 8 th Edition, Elsevier Health Sciences, 2016.
• Siegel M. Congenital malformations following chickenpox, measles, mumps, and hepatitis. Results of a cohort study. JAMA 1973;226(13):1521-4.
• World Health Organization
• Medline Plus

Exit Notification / Disclaimer Policy

• The Centers for Disease Control and Prevention (CDC) cannot attest to the accuracy of a non-federal website.
• Linking to a non-federal website does not constitute an endorsement by CDC or any of its employees of the sponsors or the information and products presented on the website.
• You will be subject to the destination website's privacy policy when you follow the link.
• CDC is not responsible for Section 508 compliance (accessibility) on other federal or private website.