Bourbon virus infection pathophysiology: Difference between revisions
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*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> | ||
*Cytokines involved in the pathogenesis of bourbon virus infection are interleukin-1, interleukin-6, interleukin-10, macrophage inflammatory protein 1, monocyte chemoattractant protein (MCP)–1, and interferon (IFN).<ref name="urlThe Interferon Antagonist ML Protein of Thogoto Virus Targets General Transcription Factor IIB">{{cite web |url=http://jvi.asm.org/content/82/22/11446.full |title=The Interferon Antagonist ML Protein of Thogoto Virus Targets General Transcription Factor IIB |format= |work= |accessdate=}}</ref> | *Cytokines involved in the pathogenesis of bourbon virus infection are interleukin-1, interleukin-6, interleukin-10, macrophage inflammatory protein 1, monocyte chemoattractant protein (MCP)–1, and interferon (IFN).<ref name="urlThe Interferon Antagonist ML Protein of Thogoto Virus Targets General Transcription Factor IIB">{{cite web |url=http://jvi.asm.org/content/82/22/11446.full |title=The Interferon Antagonist ML Protein of Thogoto Virus Targets General Transcription Factor IIB |format= |work= |accessdate=}}</ref> | ||
==Genetics== | |||
[[Image:Virus_negative_stranded.jpg|400px|align right|Negative stranded RNA virus genome replication]] | |||
==Associated conditions== | |||
==Gross Pathology== | |||
==Microscopic Pathology== | |||
Revision as of 16:56, 13 July 2017
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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
- Bourbon 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][3]
- Five larger RNA segments each encode only one gene product, the sixth segment encodes two matrix proteins, M and ML.[4]
- 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.[4]
- 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.[5]
- 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.[6][7][8][9]
- MxA recognizes the nucleocapsids of invading viruses, causing an early block of the viral replication cycle.[6][10]
- Cytokines involved in the pathogenesis of bourbon virus infection are interleukin-1, interleukin-6, interleukin-10, macrophage inflammatory protein 1, monocyte chemoattractant protein (MCP)–1, and interferon (IFN).[11]
Genetics
Associated conditions
Gross Pathology
Microscopic Pathology
References
- ↑ "Receptor-Mediated Endocytosis and the Sorting of Internalized Proteins - Molecular Cell Biology - NCBI Bookshelf".
- ↑ "www.ncbi.nlm.nih.gov" (PDF).
- ↑ Albo C, Martín J, Portela A (1996). "The 5' ends of Thogoto virus (Orthomyxoviridae) mRNAs are homogeneous in both length and sequence". J. Virol. 70 (12): 9013–7. PMC 191002. PMID 8971034.
- ↑ 4.0 4.1 "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.
- ↑ 6.0 6.1 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.
- ↑ "The Interferon Antagonist ML Protein of Thogoto Virus Targets General Transcription Factor IIB".