Open AccessIdentification of Key Residues in Virulent Canine Distemper Virus Hemagglutinin That Control CD150/SLAM-Binding Activity
Author(s) -
Ljerka Zipperle,
Johannes P. M. Langedijk,
Claes Örvell,
M. Vandevelde,
Andreas Zurbriggen,
Philippe Plattet
Publication year - 2010
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.01077-10
Subject(s) - biology , canine distemper , hemagglutinin (influenza) , paramyxoviridae , virology , morbillivirus , glycoprotein , virus , cell fusion , viral entry , virulence , sendai virus , viral envelope , microbiology and biotechnology , cell , viral replication , biochemistry , viral disease , gene
Morbillivirus cell entry is controlled by hemagglutinin (H), an envelope-anchored viral glycoprotein determining interaction with multiple host cell surface receptors. Subsequent to virus-receptor attachment, H is thought to transduce a signal triggering the viral fusion glycoprotein, which in turn drives virus-cell fusion activity. Cell entry through the universal morbillivirus receptor CD150/SLAM was reported to depend on two nearby microdomains located within the hemagglutinin. Here, we provide evidence that three key residues in the virulent canine distemper virus A75/17 H protein (Y525, D526, and R529), clustering at the rim of a large recessed groove created by beta-propeller blades 4 and 5, control SLAM-binding activity without drastically modulating protein surface expression or SLAM-independent F triggering.