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

Zipperle, Ljerka; Langedijk, J.P.; Orvell, C.; Vandevelde, Marc; Zurbriggen, Andreas; Plattet, Philippe (2010). Identification of key residues in virulent canine distemper virus hemagglutinin that control CD150/SLAM-binding activity. Journal of virology, 84(18), pp. 9618-24. Baltimore: American Society for Microbiology 10.1128/JVI.01077-10

Full text not available from this repository. (Request a copy)

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.

Item Type:

Journal Article (Original Article)

Division/Institute:

05 Veterinary Medicine > Department of Clinical Research and Veterinary Public Health (DCR-VPH) > Experimental Clinical Research
05 Veterinary Medicine > Department of Clinical Veterinary Medicine (DKV) > DKV - Clinical Neurology

UniBE Contributor:

Zipperle, Ljerka; Vandevelde, Marc; Zurbriggen, Andreas and Plattet, Philippe

ISSN:

0022-538X

Publisher:

American Society for Microbiology

Language:

English

Submitter:

Factscience Import

Date Deposited:

04 Oct 2013 14:32

Last Modified:

30 Sep 2014 14:40

Publisher DOI:

10.1128/JVI.01077-10

Web of Science ID:

000281110500061

URI:

https://boris.unibe.ch/id/eprint/12389 (FactScience: 218723)

Actions (login required)

Edit item Edit item
Provide Feedback