A mutant H3N2 influenza virus uses an alternative activation mechanism in TMPRSS2 knockout mice by loss of an oligosaccharide in the hemagglutinin stalk region.

Szczegóły
Abstrakt

Tytuł:: A mutant H3N2 influenza virus uses an alternative activation mechanism in TMPRSS2 knockout mice by loss of an oligosaccharide in the hemagglutinin stalk region.
Autorzy:: Sakai K; Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan .
Sekizuka T; Laboratory of Bacterial Genomics, Pathogen Genomics Center, National Institute of Infectious Diseases, Tokyo, Japan.
Ami Y; Division of Experimental Animal Research, National Institute of Infectious Diseases, Tokyo, Japan.
Nakajima N; Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Kitazawa M; Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan Laboratory of Animal Health, Department of Veterinary Medicine, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan.
Sato Y; Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Nakajima K; Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan Laboratory of Animal Health, Department of Veterinary Medicine, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan.
Anraku M; Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan.
Kubota T; Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan.
Komase K; Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan.
Takehara K; Laboratory of Animal Health, Department of Veterinary Medicine, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan.
Hasegawa H; Department of Pathology, National Institute of Infectious Diseases, Tokyo, Japan.
Odagiri T; Influenza Virus Research Center, National Institute of Infectious Diseases, Tokyo, Japan.
Tashiro M; Influenza Virus Research Center, National Institute of Infectious Diseases, Tokyo, Japan.
Kuroda M; Laboratory of Bacterial Genomics, Pathogen Genomics Center, National Institute of Infectious Diseases, Tokyo, Japan.
Takeda M; Department of Virology 3, National Institute of Infectious Diseases, Tokyo, Japan.
Źródło:: Journal of virology [J Virol] 2015 May; Vol. 89 (9), pp. 5154-8. Date of Electronic Publication: 2015 Feb 11.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Publication: Washington Dc : American Society For Microbiology
Original Publication: Baltimore, American Society for Microbiology.
MeSH Terms:: Protein Processing, Post-Translational*
Hemagglutinin Glycoproteins, Influenza Virus/*metabolism
Influenza A Virus, H3N2 Subtype/*genetics
Influenza A Virus, H3N2 Subtype/*physiology
Oligosaccharides/*metabolism
Serine Endopeptidases/*deficiency
Animals ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Influenza A Virus, H3N2 Subtype/growth & development ; Mice, Knockout ; Oligosaccharides/genetics ; Virulence ; Virus Internalization
References:: Virology. 1984 Dec;139(2):303-16. (PMID: 6516214)
J Virol. 2014 May;88(10):5608-16. (PMID: 24600012)
Virology. 1985 Oct 15;146(1):130-7. (PMID: 4036005)
Virology. 1986 Mar;149(2):165-73. (PMID: 3946082)
Proc Natl Acad Sci U S A. 1987 Jan;84(1):36-40. (PMID: 3467357)
Proc Natl Acad Sci U S A. 1988 Jan;85(2):324-8. (PMID: 2829180)
Virology. 1989 Feb;168(2):274-80. (PMID: 2916326)
J Virol. 1989 Aug;63(8):3296-300. (PMID: 2746732)
J Virol. 1991 Mar;65(3):1195-201. (PMID: 1847449)
Virology. 1991 Jun;182(2):475-85. (PMID: 2024485)
J Virol. 1991 Jul;65(7):3530-7. (PMID: 2041080)
J Biol Chem. 1992 Jul 5;267(19):13573-9. (PMID: 1618859)
J Immunol. 1992 Aug 1;149(3):981-8. (PMID: 1634780)
Cell. 1998 Oct 30;95(3):409-17. (PMID: 9814710)
Virology. 1999 May 25;258(1):1-20. (PMID: 10329563)
J Virol. 2006 Oct;80(19):9896-8. (PMID: 16973594)
J Virol. 2009 Apr;83(7):3200-11. (PMID: 19158246)
J Virol. 2010 May;84(10):5089-96. (PMID: 20219906)
PLoS One. 2010;5(4):e10256. (PMID: 20428231)
J Virol. 2012 Oct;86(19):10579-86. (PMID: 22811538)
PLoS Pathog. 2013 Feb;9(2):e1003151. (PMID: 23459660)
J Virol. 2013 Apr;87(8):4237-51. (PMID: 23365447)
PLoS One. 2013;8(9):e75014. (PMID: 24058646)
PLoS Pathog. 2013;9(12):e1003774. (PMID: 24348248)
J Virol. 2014 Feb;88(3):1673-83. (PMID: 24257604)
J Virol. 2014 May;88(9):4744-51. (PMID: 24522916)
EMBO J. 1984 Dec 20;3(13):3329-32. (PMID: 6526017)
Molecular Sequence:: PDB 5HMG
Substance Nomenclature:: 0 (Hemagglutinin Glycoproteins, Influenza Virus)
0 (Oligosaccharides)
EC 3.4.21.- (Serine Endopeptidases)
EC 3.4.21.- (TMPRSS2 protein, mouse)
Entry Date(s):: Date Created: 20150213 Date Completed: 20150610 Latest Revision: 20181113
Update Code:: 20240104
PubMed Central ID:: PMC4403495
DOI:: 10.1128/JVI.00124-15
PMID:: 25673722
: Czasopismo naukowe

The host protease TMPRSS2 plays an essential role in proteolytic activation of the influenza A virus (IAV) hemagglutinin (HA) protein possessing a monobasic cleavage site. However, after passages in TMPRSS2 knockout mice, an H3N2 subtype IAV began to undergo cleavage activation of HA, showing high virulence in the mice due to the loss of an oligosaccharide at position 8 in the HA stalk region. Thus, the H3N2 IAV acquired cleavability by an alternative HA activation mechanism/protease(s).
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