Bourbon virus infection pathophysiology: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 18: | Line 18: | ||
*Thogoto viruses are spherical, enveloped single stranded RNA viruses with a segmented genome. | *Thogoto viruses are spherical, enveloped single stranded RNA viruses with a segmented genome. | ||
*Virions are 80-120nm in diameter with a genome size of approximately 10Kb. The 6-7 segments of genome encodes for 7-9 proteins with each segment size ranging from a low of 0.9Kb to 2.3Kb. | *Virions are 80-120nm in diameter with a genome size of approximately 10Kb. The 6-7 segments of genome encodes for 7-9 proteins with each segment size ranging from a low of 0.9Kb to 2.3Kb. | ||
*Viral RNA polymerases (PA, PB1 and PB2) transcribe one mRNA from each gnome segment . | *Thogoto viruses differ from influenza virus in having capped viral mRNA without host messenger-derived heterogeneous sequences at the 5' end of the genome.<ref name="urlwww.ncbi.nlm.nih.gov">{{cite web |url=https://www.ncbi.nlm.nih.gov/pmc/articles/PMC192294/pdf/718347.pdf |title=www.ncbi.nlm.nih.gov |format= |work= |accessdate=}}</ref> | ||
*Splicing of segment 6 mRNA gives rise to mRNA coding for the matrix protein M1. | *Five larger RNA segments each encode only one gene product, the sixth segment encodes two matrix proteins, M and ML.<ref name="urlMicrobiology Society Journals | Functional comparison of the two gene products of Thogoto virus segment 6">{{cite web |url=http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80300-0#tab2 |title=Microbiology Society Journals | Functional comparison of the two gene products of Thogoto virus segment 6 |format= |work= |accessdate=}}</ref> | ||
*Viral RNA polymerases (PA, PB1 and PB2) transcribe one mRNA from each gnome segment. | |||
*Splicing of segment 6 mRNA gives rise to mRNA coding for the matrix protein M1.<ref name="urlMicrobiology Society Journals | Functional comparison of the two gene products of Thogoto virus segment 6">{{cite web |url=http://jgv.microbiologyresearch.org/content/journal/jgv/10.1099/vir.0.80300-0#tab2 |title=Microbiology Society Journals | Functional comparison of the two gene products of Thogoto virus segment 6 |format= |work= |accessdate=}}</ref> | |||
*Transcription of genomic segments by the viral polymerase produces mRNAs that are capped and polyadenylated by the viral polymerase. | *Transcription of genomic segments by the viral polymerase produces mRNAs that are capped and polyadenylated by the viral polymerase. | ||
*The M1 protein is involved in export of genome from the nucleus. | *The M1 protein is involved in export of genome from the nucleus. | ||
| Line 26: | Line 28: | ||
*Thogoto Virus Infection induces a sustained type 1 interferon response in the host until the daptive immunity takes effect.<ref name="pmid20861272">{{cite journal |vauthors=Kochs G, Bauer S, Vogt C, Frenz T, Tschopp J, Kalinke U, Waibler Z |title=Thogoto virus infection induces sustained type I interferon responses that depend on RIG-I-like helicase signaling of conventional dendritic cells |journal=J. Virol. |volume=84 |issue=23 |pages=12344–50 |year=2010 |pmid=20861272 |pmc=2976394 |doi=10.1128/JVI.00931-10 |url=}}</ref> | *Thogoto Virus Infection induces a sustained type 1 interferon response in the host until the daptive immunity takes effect.<ref name="pmid20861272">{{cite journal |vauthors=Kochs G, Bauer S, Vogt C, Frenz T, Tschopp J, Kalinke U, Waibler Z |title=Thogoto virus infection induces sustained type I interferon responses that depend on RIG-I-like helicase signaling of conventional dendritic cells |journal=J. Virol. |volume=84 |issue=23 |pages=12344–50 |year=2010 |pmid=20861272 |pmc=2976394 |doi=10.1128/JVI.00931-10 |url=}}</ref> | ||
*IFN expression is mediated by specialized plasmacytoid dendritic cells (pDC). | *IFN expression is mediated by specialized plasmacytoid dendritic cells (pDC). | ||
*The interferon-induced dynamin-like MxA protein is involved in host antiviral activity against thogoto viruses.<ref name="pmid24448803">{{cite journal |vauthors=Patzina C, Haller O, Kochs G |title=Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus |journal=J. Biol. Chem. |volume=289 |issue=9 |pages=6020–7 |year=2014 |pmid=24448803 |pmc=3937669 |doi=10.1074/jbc.M113.543892 |url=}}</ref><ref name="pmid21166595">{{cite journal |vauthors=Haller O, Kochs G |title=Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity |journal=J. Interferon Cytokine Res. |volume=31 |issue=1 |pages=79–87 |year=2011 |pmid=21166595 |doi=10.1089/jir.2010.0076 |url=}}</ref><ref name="pmid7745744">{{cite journal |vauthors=Frese M, Kochs G, Meier-Dieter U, Siebler J, Haller O |title=Human MxA protein inhibits tick-borne Thogoto virus but not Dhori virus |journal=J. Virol. |volume=69 |issue=6 |pages=3904–9 |year=1995 |pmid=7745744 |pmc=189115 |doi= |url=}}</ref> | *The interferon-induced dynamin-like MxA protein is involved in host antiviral activity against thogoto viruses.<ref name="pmid24448803">{{cite journal |vauthors=Patzina C, Haller O, Kochs G |title=Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus |journal=J. Biol. Chem. |volume=289 |issue=9 |pages=6020–7 |year=2014 |pmid=24448803 |pmc=3937669 |doi=10.1074/jbc.M113.543892 |url=}}</ref><ref name="pmid21166595">{{cite journal |vauthors=Haller O, Kochs G |title=Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity |journal=J. Interferon Cytokine Res. |volume=31 |issue=1 |pages=79–87 |year=2011 |pmid=21166595 |doi=10.1089/jir.2010.0076 |url=}}</ref><ref name="pmid7745744">{{cite journal |vauthors=Frese M, Kochs G, Meier-Dieter U, Siebler J, Haller O |title=Human MxA protein inhibits tick-borne Thogoto virus but not Dhori virus |journal=J. Virol. |volume=69 |issue=6 |pages=3904–9 |year=1995 |pmid=7745744 |pmc=189115 |doi= |url=}}</ref><ref name="pmid8992952">{{cite journal |vauthors=Pringle CR |title=Virus taxonomy 1996 - a bulletin from the Xth International Congress of Virology in Jerusalem |journal=Arch. Virol. |volume=141 |issue=11 |pages=2251–6 |year=1996 |pmid=8992952 |doi= |url=}}</ref> | ||
*MxA recognizes the nucleocapsids of invading viruses, causing an early block of the viral replication cycle.<ref name="pmid24448803">{{cite journal |vauthors=Patzina C, Haller O, Kochs G |title=Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus |journal=J. Biol. Chem. |volume=289 |issue=9 |pages=6020–7 |year=2014 |pmid=24448803 |pmc=3937669 |doi=10.1074/jbc.M113.543892 |url=}}</ref><ref name="pmid1548781">{{cite journal |vauthors=Pavlovic J, Haller O, Staeheli P |title=Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle |journal=J. Virol. |volume=66 |issue=4 |pages=2564–9 |year=1992 |pmid=1548781 |pmc=289059 |doi= |url=}}</ref> | *MxA recognizes the nucleocapsids of invading viruses, causing an early block of the viral replication cycle.<ref name="pmid24448803">{{cite journal |vauthors=Patzina C, Haller O, Kochs G |title=Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus |journal=J. Biol. Chem. |volume=289 |issue=9 |pages=6020–7 |year=2014 |pmid=24448803 |pmc=3937669 |doi=10.1074/jbc.M113.543892 |url=}}</ref><ref name="pmid1548781">{{cite journal |vauthors=Pavlovic J, Haller O, Staeheli P |title=Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle |journal=J. Virol. |volume=66 |issue=4 |pages=2564–9 |year=1992 |pmid=1548781 |pmc=289059 |doi= |url=}}</ref> | ||
Revision as of 16:35, 13 July 2017
|
Bourbon virus infection Microchapters |
|
Diagnosis |
|---|
|
Treatment |
|
Case Studies |
|
Bourbon virus infection pathophysiology On the Web |
|
American Roentgen Ray Society Images of Bourbon virus infection pathophysiology |
|
Risk calculators and risk factors for Bourbon virus infection pathophysiology |
Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]; Associate Editor(s)-in-Chief: Syed Hassan A. Kazmi BSc, MD [2]
Overview
Pathophysiology
Bourbon virus is a negative sense segmented RNA virus belonging to the genus Thogotovirus, family Orthomyxovirida.
Transmission
- Boubon virus is transmitted mainly by ticks.
- The virus is able to replicate in vertebrate and tick cells.
Adherence
- Virus attaches to the N-acetylneuraminic acid component found in host cell membrane (sialic acid receptors).[1]
Endocytosis
- The virus gets endocytosed by clathrins into the host cell.
- Endosome acidification induces fusion of virus membrane with the vesicle membrane.
Virology and replication
- Thogoto viruses are spherical, enveloped single stranded RNA viruses with a segmented genome.
- Virions are 80-120nm in diameter with a genome size of approximately 10Kb. The 6-7 segments of genome encodes for 7-9 proteins with each segment size ranging from a low of 0.9Kb to 2.3Kb.
- Thogoto viruses differ from influenza virus in having capped viral mRNA without host messenger-derived heterogeneous sequences at the 5' end of the genome.[2]
- Five larger RNA segments each encode only one gene product, the sixth segment encodes two matrix proteins, M and ML.[3]
- Viral RNA polymerases (PA, PB1 and PB2) transcribe one mRNA from each gnome segment.
- Splicing of segment 6 mRNA gives rise to mRNA coding for the matrix protein M1.[3]
- Transcription of genomic segments by the viral polymerase produces mRNAs that are capped and polyadenylated by the viral polymerase.
- The M1 protein is involved in export of genome from the nucleus.
- Assembly of the virus takes place in the cytoplasm from where new virions are released to infect other cells.
Host response
- Thogoto Virus Infection induces a sustained type 1 interferon response in the host until the daptive immunity takes effect.[4]
- IFN expression is mediated by specialized plasmacytoid dendritic cells (pDC).
- The interferon-induced dynamin-like MxA protein is involved in host antiviral activity against thogoto viruses.[5][6][7][8]
- MxA recognizes the nucleocapsids of invading viruses, causing an early block of the viral replication cycle.[5][9]
References
- ↑ "Receptor-Mediated Endocytosis and the Sorting of Internalized Proteins - Molecular Cell Biology - NCBI Bookshelf".
- ↑ "www.ncbi.nlm.nih.gov" (PDF).
- ↑ 3.0 3.1 "Microbiology Society Journals | Functional comparison of the two gene products of Thogoto virus segment 6".
- ↑ Kochs G, Bauer S, Vogt C, Frenz T, Tschopp J, Kalinke U, Waibler Z (2010). "Thogoto virus infection induces sustained type I interferon responses that depend on RIG-I-like helicase signaling of conventional dendritic cells". J. Virol. 84 (23): 12344–50. doi:10.1128/JVI.00931-10. PMC 2976394. PMID 20861272.
- ↑ 5.0 5.1 Patzina C, Haller O, Kochs G (2014). "Structural requirements for the antiviral activity of the human MxA protein against Thogoto and influenza A virus". J. Biol. Chem. 289 (9): 6020–7. doi:10.1074/jbc.M113.543892. PMC 3937669. PMID 24448803.
- ↑ Haller O, Kochs G (2011). "Human MxA protein: an interferon-induced dynamin-like GTPase with broad antiviral activity". J. Interferon Cytokine Res. 31 (1): 79–87. doi:10.1089/jir.2010.0076. PMID 21166595.
- ↑ Frese M, Kochs G, Meier-Dieter U, Siebler J, Haller O (1995). "Human MxA protein inhibits tick-borne Thogoto virus but not Dhori virus". J. Virol. 69 (6): 3904–9. PMC 189115. PMID 7745744.
- ↑ Pringle CR (1996). "Virus taxonomy 1996 - a bulletin from the Xth International Congress of Virology in Jerusalem". Arch. Virol. 141 (11): 2251–6. PMID 8992952.
- ↑ Pavlovic J, Haller O, Staeheli P (1992). "Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle". J. Virol. 66 (4): 2564–9. PMC 289059. PMID 1548781.