Aromatic amino acids in the juxtamembrane domain of severe acute respiratory syndrome coronavirus spike glycoprotein are important for receptor-dependent virus entry and cell-cell fusion

Journal of Virology
Megan W HowardKathryn V Holmes

Abstract

The severe acute respiratory syndrome coronavirus (SARS-CoV) spike glycoprotein (S) is a class I viral fusion protein that binds to its receptor glycoprotein, human angiotensin converting enzyme 2 (hACE2), and mediates virus entry and cell-cell fusion. The juxtamembrane domain (JMD) of S is an aromatic amino acid-rich region proximal to the transmembrane domain that is highly conserved in all coronaviruses. Alanine substitutions for one or two of the six aromatic residues in the JMD did not alter the surface expression of the SARS-CoV S proteins with a deletion of the C-terminal 19 amino acids (S Delta19) or reduce binding to soluble human ACE2 (hACE2). However, hACE2-dependent entry of trypsin-treated retrovirus pseudotyped viruses expressing JMD mutant S Delta19 proteins was greatly reduced. Single alanine substitutions for aromatic residues reduced entry to 10 to 60% of the wild-type level. The greatest reduction was caused by residues nearest the transmembrane domain. Four double alanine substitutions reduced entry to 5 to 10% of the wild-type level. Rapid hACE2-dependent S-mediated cell-cell fusion was reduced to 60 to 70% of the wild-type level for all single alanine substitutions and the Y1188A/Y1191A protein. S Delta19 ...Continue Reading

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Citations

Jul 21, 2012·Viruses·Sandrine BelouzardGary R Whittaker
Mar 5, 2016·Traffic·Judith M White, Gary R Whittaker
Jun 24, 2008·Critical Reviews in Biochemistry and Molecular Biology·Judith M WhiteKathryn Schornberg
Jan 1, 2016·Toxicology and Environmental Health Sciences·Simranjeet Singh SekhonYang-Hoon Kim
Apr 13, 2021·Virus Research·Thalia Rodriguez, Hana M Dobrovolny
Apr 12, 2020·The Science of the Total Environment·Balachandar VellingiriMohana Devi Subramaniam

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