Title :

Structural and functional analysis of natural capsid variants suggests sialic acid-independent entry of BK polyomavirus

Author(s) :

Sorin, Marie N [Auteur]
Di Maio, Antonio [Auteur]
Silva, Lisete M [Auteur]
Ebert, Domenic [Auteur]
Delannoy, Clément [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Nguyen, Ngoc-Khanh [Auteur]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Gifu University
Chai, Wengang [Auteur]
Halary, Franck [Auteur]
Renaudin-Autain, Karine [Auteur]
Liu, Yan [Auteur]
Bressollette-Bodin, Céline [Auteur]
Stehle, Thilo [Auteur]
McIlroy, Dorian [Auteur]

Journal title :

Cell Reports

Abbreviated title :

Cell Rep

Volume number :

42

Pages :

112114

Publisher :

Elsevier

Publication date :

2023-02-14

ISSN :

2211-1247

English keyword(s) :

CP: Microbiology
CP: Molecular biology
capsid
glycan
polyomavirus
receptor
structure
tropism

HAL domain(s) :

Sciences du Vivant [q-bio]
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
Sciences du Vivant [q-bio]/Microbiologie et Parasitologie/Virologie
Chimie/Chimie théorique et/ou physique

English abstract : [en]

BK polyomavirus (BKPyV) is an opportunistic pathogen that uses the b-series gangliosides GD1b and GT1b as entry receptors. Here, we characterize the impact of naturally occurring VP1 mutations on ganglioside binding, VP1 ...
Show more >BK polyomavirus (BKPyV) is an opportunistic pathogen that uses the b-series gangliosides GD1b and GT1b as entry receptors. Here, we characterize the impact of naturally occurring VP1 mutations on ganglioside binding, VP1 protein structure, and virus tropism. Infectious entry of single mutants E73Q and E73A and the triple mutant A72V-E73Q-E82Q (VQQ) remains sialic acid dependent, and all three variants acquire binding to a-series gangliosides, including GD1a. However, the E73A and VQQ variants lose the ability to infect ganglioside-complemented cells, and this correlates with a clear shift of the BC2 loop in the crystal structures of E73A and VQQ. On the other hand, the K69N mutation in the K69N-E82Q variant leads to a steric clash that precludes sialic acid binding. Nevertheless, this mutant retains significant infectivity in 293TT cells, which is not dependent on heparan sulfate proteoglycans, implying that an unknown sialic acid-independent entry receptor for BKPyV exists.Show less >

Language :

Anglais

Peer reviewed article :

Oui

Audience :

Internationale

Popular science :

Non

ANR Project :

Evolution génétique virale et anticorps neutralisants au cours des infections à polyomavirus BK: vers une nouvelle stratégie thérapeutique

Administrative institution(s) :

Université de Lille
CNRS

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

Chemical Glycobiology

Submission date :

2023-07-19T08:51:29Z
2023-09-01T14:23:47Z