Structural and functional analysis of ...
Document type :
Article dans une revue scientifique
PMID :
Permalink :
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 P [Auteur]
Nguyen, Ngoc-Khanh [Auteur]
Guerardel, Yann [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Chai, Wengang [Auteur]
Halary, Franck [Auteur]
Renaudin-Autain, Karine [Auteur]
Liu, Yan [Auteur]
Bressollette-Bodin, Céline [Auteur]
Stehle, Thilo [Auteur]
McIlroy, Dorian [Auteur]
Di Maio, Antonio [Auteur]
Silva, Lisete M [Auteur]
Ebert, Domenic [Auteur]
Delannoy, Clément P [Auteur]
Nguyen, Ngoc-Khanh [Auteur]
Guerardel, Yann [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
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
Publication date :
2023-02-14
ISSN :
2211-1247
English keyword(s) :
CP: Microbiology
CP: Molecular biology
capsid
glycan
polyomavirus
receptor
structure
tropism
CP: Molecular biology
capsid
glycan
polyomavirus
receptor
structure
tropism
HAL domain(s) :
Sciences du Vivant [q-bio]
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 >
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
Audience :
Non spécifiée
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Chemical Glycobiology
Submission date :
2023-07-19T08:51:29Z
Files
- P23.21 Sorin 2023 Cell reports.pdf
- Version éditeur
- Open access
- Access the document