Open AccessTMPRSS2 Is an Activating Protease for Respiratory Parainfluenza Viruses
Author(s) -
Masako Abe,
Maino Tahara,
Kouji Sakai,
Hiromi Yamaguchi,
Kazuhiko Kanou,
Kazuya Shirato,
Miyuki Kawase,
Masahiro Noda,
Hirokazu Kimura,
Shutoku Matsuyama,
Hideo Fukuhara,
Katsumi Mizuta,
Katsumi Maenaka,
Yasushi Ami,
Mariko Esumi,
Atsushi Kato,
Makoto Takeda
Publication year - 2013
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.01490-13
Subject(s) - biology , sendai virus , tmprss2 , virology , respiratory system , viral replication , serine protease , glutamine , protease , proteases , virus , enzyme , biochemistry , covid-19 , amino acid , disease , medicine , pathology , infectious disease (medical specialty) , anatomy
Here, we show that human parainfluenza viruses and Sendai virus (SeV), like other respiratory viruses, use TMPRSS2 for their activation. The membrane fusion proteins of respiratory viruses often possess serine and glutamine residues at the P2 and P3 positions, respectively, but these residues were not critical for cleavage by TMPRSS2. However, mutations of these residues affected SeV growth in specific epithelial cell lines, suggesting the importance of these residues for SeV replication in epithelia.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom