Identification of key residues in virulent canine distemper virus hemagglutinin that control CD150/SLAM-binding activity.

Journal of Virology
Ljerka ZipperlePhilippe Plattet

Abstract

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.

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Citations

Oct 19, 2012·Journal of Virology·Nadine AderPhilippe Plattet
May 23, 2012·Comparative Immunology, Microbiology and Infectious Diseases·Se-Yeoun ChaHyung-Kwan Jang
Nov 2, 2011·The Veterinary Clinics of North America. Small Animal Practice·Sanjay Kapil, Teresa J Yeary
Aug 16, 2011·Veterinary Microbiology·Yuki KameoKen Maeda
Feb 15, 2014·Current Opinion in Virology·Martin LudlowW Paul Duprex
Jul 25, 2015·BMC Veterinary Research·Guan-Ming KePei-Yu Chu
Jan 22, 2005·Veterinary Immunology and Immunopathology·Martina SchobesbergerChristian Griot
Dec 3, 2016·The Journal of General Virology·Angelika K LootsEstelle H Venter
Nov 27, 2015·Journal of Virology·Mojtaba KhosraviPhilippe Plattet
Mar 20, 2015·Journal of Virology·Lisa AlvesPhilippe Plattet
Mar 16, 2019·The Journal of General Virology·Chen ChenLing Zhao
Jul 15, 2016·Clinical Microbiology Reviews·Pablo F CéspedesSusan M Bueno
Jun 24, 2021·Scientific Reports·Vivaldo Gomes da CostaRicardo Henrique Krüger

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