Host serine proteases TMPRSS2 and TMPRSS11D mediate proteolytic activation and trypsin-independent infection in group A rotaviruses

Sasaki, Michihito; Itakura, Yukari; Kishimoto, Mai; Tabata, Koshiro; Uemura, Kentaro; Ito, Naoto; Sugiyama, Makoto; Wastika, Christida E; Orba, Yasuko; Sawa, Hirofumi

Host serine proteases TMPRSS2 and TMPRSS11D mediate proteolytic activation and trypsin-independent infection in group A rotaviruses

Sasaki, Michihito; Itakura, Yukari; Kishimoto, Mai et al.

Journal of virology, 2021, 95(11), e00398-21

Permalink : https://hdl.handle.net/2115/81748

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アクセス権	open access
URI	https://hdl.handle.net/2115/81748
タイトル	Host serine proteases TMPRSS2 and TMPRSS11D mediate proteolytic activation and trypsin-independent infection in group A rotaviruses
著者	Sasaki, Michihito ; Itakura, Yukari ; Kishimoto, Mai ; Tabata, Koshiro ; Uemura, Kentaro ; Ito, Naoto ; Sugiyama, Makoto ; Wastika, Christida E ; Orba, Yasuko ; Sawa, Hirofumi
e-Rad_Researcher 70609403 著者名 Sasaki, Michihito
著者名 Itakura, Yukari
著者名 Kishimoto, Mai
著者名 Tabata, Koshiro
著者名 Uemura, Kentaro
e-Rad_Researcher 20334922 著者名 Ito, Naoto
e-Rad_Researcher 80196774 著者名 Sugiyama, Makoto
著者名 Wastika, Christida E
e-Rad_Researcher 60507169 著者名 Orba, Yasuko
e-Rad_Researcher 30292006 著者名 Sawa, Hirofumi
言語	英語
キーワード	group A rotavirus
	proteolytic activation
	type II transmembrane serine proteases
	VP4
	viral entry
発行日	2021-06
出版者	American Society for Microbiology
収録物名	Journal of virology
巻(号)	95(11)
ページ	e00398-21
抄録	Group A rotaviruses (RVAs) are representative enteric virus species and major causes of diarrhea in humans and animals. The RVA virion is a triple-layered particle, and the outermost layer consists of the glycoprotein VP7 and spike protein VP4. To increase the infectivity of RVA, VP4 is proteolytically cleaved into VP5* and VP8* subunits by trypsin; these subunits form a rigid spike structure on the virion surface. In this study, we investigated the growth of RVAs in cells transduced with type II transmembrane serine proteases (TTSPs), which cleave fusion proteins and promote infection by respiratory viruses, such as influenza viruses, paramyxoviruses, and coronaviruses. We identified TMPRSS2 and TMPRSS11D as host TTSPs that mediate trypsin-independent and multicycle infection by human and animal RVA strains. In vitro cleavage assays revealed that recombinant TMPRSS11D cleaved RVA VP4. We also found that TMPRSS2 and TMPRSS11D promote the infectious entry of immature RVA virions, but they could not activate nascent progeny virions in the late phase of infection. This observation differed from the TTSP-mediated activation process of paramyxoviruses, revealing the existence of virus species-specific activation processes in TTSPs. Our study provides new insights into the interaction between RVAs and host factors, and TTSP-transduced cells offer potential advantages for RVA research and development.
資源タイプ	学術雑誌論文
出版タイプ	Version of Record
PISSN	0022-538X
EISSN	1098-5514
NCID	AA12024806
関連情報	PMID 33762412
関連情報 (isIdenticalTo)	出版社版DOI https://doi.org/10.1128/JVI.00398-21