Mumps pathophysiology: Difference between revisions
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{{Mumps}} | {{Mumps}} | ||
{{CMG}}; {{AOEIC}} {{LG}} | {{CMG}}; {{AOEIC}} {{LG}}; {{NRM}} | ||
==Overview== | ==Overview== | ||
Humans are the only natural host for mumps virus (MuV). MuV is transmitted through respiratory droplets (saliva or mucus), direct contact, or contact with surfaces carrying MuV. MuV infects the [[upper respiratory tract]] [[epithelium]] by binding to extracellular [[sialic acid]] via the hemagglutinin-neuraminidase (HN) [[glycoprotein]]. MuV is able to evade an immune response with small hydrophobic (SH) protein, which blocks [[Tumor necrosis factor-alpha|TNFα-mediated apoptosis]], and with the V proteins, which inhibit [[IFN]] production and signaling. MuV disseminates through the [[lymphatic system]] to cause systemic infection. Replication in the [[parotid gland]] (or other salivary gland) causes [[mononuclear cell]] infiltration, [[hemorrhage]], [[edema]], and [[necrosis]]. | |||
==Pathophysiology== | ==Pathophysiology== | ||
===Transmission=== | ===Transmission=== | ||
* | *Humans are the only natural host for mumps virus (MuV). | ||
*MuV is transmitted through respiratory droplets (saliva or mucus), direct contact, or contact with surfaces carrying MuV. | |||
* | *Mumps is contagious several days prior and up to 5 days after onset of [[parotitis]]. | ||
===Pathogenesis=== | ===Pathogenesis=== | ||
*MuV enters the body through inhalation or oral contact and infects the [[upper respiratory tract]] [[epithelium]].<ref name="pmid25229387">{{cite journal| author=Rubin S, Eckhaus M, Rennick LJ, Bamford CG, Duprex WP| title=Molecular biology, pathogenesis and pathology of mumps virus. | journal=J Pathol | year= 2015 | volume= 235 | issue= 2 | pages= 242-52 | pmid=25229387 | doi=10.1002/path.4445 | pmc=PMC4268314 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=25229387 }} </ref> | |||
*MuV is able to attach to extracellular [[sialic acid]] via the hemagglutinin-neuraminidase (HN) [[glycoprotein]]. | |||
*HN and the fusion (F) glycoprotein mediate cell membrane fusion, allowing viral material to enter respiratory [[Epithelium|epithelial cells]]. | |||
*HN and F, in conjunction with matrix (M) protein, are also involved in localizing viral material after replication and inducing [[virion]] budding. | |||
*MuV is able to inhibit an immune response to infection with the following [[Virulence factor|virulence factors]]: | |||
:*Small hydrophobic (SH) protein is presumed to block [[Tumor necrosis factor-alpha|TNFα-mediated apoptosis]].<ref name="pmid11287556">{{cite journal| author=He B, Lin GY, Durbin JE, Durbin RK, Lamb RA| title=The SH integral membrane protein of the paramyxovirus simian virus 5 is required to block apoptosis in MDBK cells. | journal=J Virol | year= 2001 | volume= 75 | issue= 9 | pages= 4068-79 | pmid=11287556 | doi=10.1128/JVI.75.9.4068-4079.2001 | pmc=PMC114152 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=11287556 }} </ref> | |||
:*Non-structural proteins NS1 and NS2 (V proteins) inhibit [[IFN]] production and signaling.<ref name="pmid15563593">{{cite journal| author=Andrejeva J, Childs KS, Young DF, Carlos TS, Stock N, Goodbourn S et al.| title=The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter. | journal=Proc Natl Acad Sci U S A | year= 2004 | volume= 101 | issue= 49 | pages= 17264-9 | pmid=15563593 | doi=10.1073/pnas.0407639101 | pmc=PMC535396 | url=http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=15563593 }} </ref> | |||
*MuV disseminates through the [[lymphatic system]] to cause systemic infection. | |||
*Replication in the [[parotid gland]] (or other salivary gland) causes [[mononuclear cell]] infiltration, [[hemorrhage]], [[edema]], and [[necrosis]]. | |||
== | ====Virulence Factors==== | ||
*Small hydrophobic (SH) protein: blocks TNFα-mediated apoptosis | |||
== | *Non-structural proteins NS1 and NS2 (V proteins): inhibit IFN production and signaling | ||
*Haemagglutinin-neuraminidase (HN) glycoprotein: binds with extracellular host cell sialic acid | |||
==Resources== | ==Resources== | ||
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[[Category:Disease]] | [[Category:Disease]] | ||
[[Category:Pediatrics]] | [[Category:Pediatrics]] | ||
[[Category:Dermatology]] | [[Category:Dermatology]] | ||
Latest revision as of 18:07, 18 September 2017
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Mumps Microchapters |
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Mumps pathophysiology On the Web |
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American Roentgen Ray Society Images of Mumps pathophysiology |
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
Humans are the only natural host for mumps virus (MuV). MuV is transmitted through respiratory droplets (saliva or mucus), direct contact, or contact with surfaces carrying MuV. MuV infects the upper respiratory tract epithelium by binding to extracellular sialic acid via the hemagglutinin-neuraminidase (HN) glycoprotein. MuV is able to evade an immune response with small hydrophobic (SH) protein, which blocks TNFα-mediated apoptosis, and with the V proteins, which inhibit IFN production and signaling. MuV disseminates through the lymphatic system to cause systemic infection. Replication in the parotid gland (or other salivary gland) causes mononuclear cell infiltration, hemorrhage, edema, and necrosis.
Pathophysiology
Transmission
- Humans are the only natural host for mumps virus (MuV).
- MuV is transmitted through respiratory droplets (saliva or mucus), direct contact, or contact with surfaces carrying MuV.
- Mumps is contagious several days prior and up to 5 days after onset of parotitis.
Pathogenesis
- MuV enters the body through inhalation or oral contact and infects the upper respiratory tract epithelium.[1]
- MuV is able to attach to extracellular sialic acid via the hemagglutinin-neuraminidase (HN) glycoprotein.
- HN and the fusion (F) glycoprotein mediate cell membrane fusion, allowing viral material to enter respiratory epithelial cells.
- HN and F, in conjunction with matrix (M) protein, are also involved in localizing viral material after replication and inducing virion budding.
- MuV is able to inhibit an immune response to infection with the following virulence factors:
- Small hydrophobic (SH) protein is presumed to block TNFα-mediated apoptosis.[2]
- Non-structural proteins NS1 and NS2 (V proteins) inhibit IFN production and signaling.[3]
- MuV disseminates through the lymphatic system to cause systemic infection.
- Replication in the parotid gland (or other salivary gland) causes mononuclear cell infiltration, hemorrhage, edema, and necrosis.
Virulence Factors
- Small hydrophobic (SH) protein: blocks TNFα-mediated apoptosis
- Non-structural proteins NS1 and NS2 (V proteins): inhibit IFN production and signaling
- Haemagglutinin-neuraminidase (HN) glycoprotein: binds with extracellular host cell sialic acid
Resources
References
- ↑ 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.
- ↑ 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.
- ↑ 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.