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N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity

Journal of general virology, 2020-06, Vol.101 (6), p.599-608 [Peer Reviewed Journal]

2020 The Authors 2020 ;ISSN: 0022-1317 ;EISSN: 1465-2099 ;DOI: 10.1099/jgv.0.001408 ;PMID: 32213247

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Title:
N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity
Author: Bouwman, K M ; Habraeken, N ; Laconi, A ; Berends, A J ; Groenewoud, L ; Alders, M ; Kemp, V ; Verheije, M H
Subjects: Animals ; Cell Line ; Chick Embryo ; Coronavirus Infections - immunology ; Coronavirus Infections - virology ; Glycosylation ; Host Specificity - immunology ; Infectious bronchitis virus - chemistry ; Infectious bronchitis virus - immunology ; Kidney - cytology ; Kidney - embryology ; Protein Binding ; Protein Domains ; Receptors, Cell Surface - metabolism ; Receptors, Virus - immunology ; Receptors, Virus - metabolism ; Recombinant Proteins ; Spike Glycoprotein, Coronavirus - chemistry ; Spike Glycoprotein, Coronavirus - metabolism ; Viral Tropism - immunology ; Virus Attachment ; Virus Replication
Is Part Of: Journal of general virology, 2020-06, Vol.101 (6), p.599-608
Description: Infection of chicken coronavirus infectious bronchitis virus (IBV) is initiated by binding of the viral heavily N-glycosylated attachment protein spike to the alpha-2,3-linked sialic acid receptor Neu5Ac. Previously, we have shown that N-glycosylation of recombinantly expressed receptor binding domain (RBD) of the spike of IBV-M41 is of critical importance for binding to chicken trachea tissue. Here we investigated the role of N-glycosylation of the RBD on receptor specificity and virus replication in the context of the virus particle. Using our reverse genetics system we were able to generate recombinant IBVs for nine-out-of-ten individual N-glycosylation mutants. growth kinetics of these viruses were comparable to the virus containing the wild-type M41-S1. Furthermore, Neu5Ac binding by the recombinant viruses containing single N-glycosylation site knock-out mutations matched the Neu5Ac binding observed with the recombinant RBDs. Five N-glycosylation mutants lost the ability to bind Neu5Ac and gained binding to a different, yet unknown, sialylated glycan receptor on host cells. These results demonstrate that N-glycosylation of IBV is a determinant for receptor specificity.
Publisher: England: Microbiology Society
Language: English
Identifier: ISSN: 0022-1317
EISSN: 1465-2099
DOI: 10.1099/jgv.0.001408
PMID: 32213247
Source: GFMER Free Medical Journals
MEDLINE
Alma/SFX Local Collection

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N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity

2020 The Authors 2020 ;ISSN: 0022-1317 ;EISSN: 1465-2099 ;DOI: 10.1099/jgv.0.001408 ;PMID: 32213247

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