Mumps virus

(Redirected from Mumps causes)
Jump to navigation Jump to search

Mumps Microchapters

Home

Patient Information

Overview

Historical Perspective

Pathophysiology

Causes

Differentiating Mumps from other Diseases

Epidemiology and Demographics

Risk Factors

Natural History, Complications and Prognosis

Diagnosis

Diagnostic Criteria

History and Symptoms

Physical Examination

Laboratory Findings

CT

Ultrasound

Other Imaging Findings

Other Diagnostic Studies

Treatment

Medical Therapy

Primary Prevention

Secondary Prevention

Cost-Effectiveness of Therapy

Future or Investigational Therapies

Case Studies

Case #1

Mumps virus On the Web

Most recent articles

Most cited articles

Review articles

CME Programs

Powerpoint slides

Images

American Roentgen Ray Society Images of Mumps virus

All Images
X-rays
Echo & Ultrasound
CT Images
MRI

Ongoing Trials at Clinical Trials.gov

US National Guidelines Clearinghouse

NICE Guidance

FDA on Mumps virus

CDC on Mumps virus

Mumps virus in the news

Blogs on Mumps virus

Directions to Hospitals Treating Mumps

Risk calculators and risk factors for Mumps virus

style="background:#Template:Taxobox colour;"|Template:Taxobox name
TEM micrograph of the mumps virus.
TEM micrograph of the mumps virus.
style="background:#Template:Taxobox colour;" | Virus classification
Group: Group V ((-)ssRNA)
Order: Mononegavirales
Family: Paramyxoviridae
Genus: Rubulavirus
Type species
Mumps virus

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-In-Chief: Lakshmi Gopalakrishnan, M.B.B.S. [2]; Nate Michalak, B.A.

Overview

Mumps virus (MuV) is an enveloped, non-segmented, negative-sense RNA virus that causes mumps. MuV belongs to the genus Rubulavirus and family Paramyxovirus. Humans are the only natural host of MuV. MuV is transmitted through respiratory droplets (saliva or mucus), direct contact, or contact with surfaces carrying MuV. MuV is able to bind to host epithelial cells via haemagglutinin-neuraminidase (HN) and fusion (F) glycoproteins. Small hydrophobic (SH) protein is presumed to block TNFα-mediated apoptosis. Non-structural proteins NS1 and NS2 (V proteins) inhibit IFN production and signaling.

Organism

Morphology

  • The spherical virion is approximately 200nm is diameter and its genome consists of a single RNA strand of 15,384 nucleotides.[2]
  • The RNA is encapsidated by nucleoprotein (N protein) forming the ribonucleoprotein (RNP) complex.

Replication Cycle

  • MuV binds to host cell sialic acid via haemagglutinin-neuraminidase (HN) and fusion (F) glycoproteins and cause virus-to-cell membrane fusion.
  • Replication and transcription is mediated by an RNA polymerase complex composed of large (L) and phospho- (P) proteins.
  • Budding is initiated after HN and F glycoproteins are transported through the endoplasmic reticulum and Golgi body to the cell surface.
  • Matrix (M) protein localizes the RNP to the area of the host cell expressing HN and F.

Human Pathogen

  • Humans are the only natural host of MuV.
  • MuV is transmitted through respiratory droplets (saliva or mucus), direct contact, or contact with surfaces carrying MuV.
  • MuV is able to evade an immune response to infection with the following virulence factors:
  • Small hydrophobic (SH) protein is presumed to block TNFα-mediated apoptosis.[3]
  • Non-structural proteins NS1 and NS2 (V proteins) inhibit IFN production and signaling.[4]

Related Chapters

References

  1. Rubin S, Eckhaus M, Rennick LJ, Bamford CG, Duprex WP (2015). "Molecular biology, pathogenesis and pathology of mumps virus". J Pathol. 235 (2): 242–52. doi:10.1002/path.4445. PMC 4268314. PMID 25229387.
  2. Hviid A, Rubin S, Mühlemann K (March 2008). "Mumps". The Lancet. 371 (9616): 932–44. doi:10.1016/S0140-6736(08)60419-5. PMID 18342688.
  3. He B, Lin GY, Durbin JE, Durbin RK, Lamb RA (2001). "The SH integral membrane protein of the paramyxovirus simian virus 5 is required to block apoptosis in MDBK cells". J Virol. 75 (9): 4068–79. doi:10.1128/JVI.75.9.4068-4079.2001. PMC 114152. PMID 11287556.
  4. Andrejeva J, Childs KS, Young DF, Carlos TS, Stock N, Goodbourn S; et al. (2004). "The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter". Proc Natl Acad Sci U S A. 101 (49): 17264–9. doi:10.1073/pnas.0407639101. PMC 535396. PMID 15563593.


Template:WikiDoc Sources