About: covid:ann/target/cdd27de1e887a76615a1be0e0bf6e02a6da7e182

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About: covid:ann/target/cdd27de1e887a76615a1be0e0bf6e02a6da7e182 Goto Sponge NotDistinct Permalink

An Entity of Type : owl:Thing, within Data Space : covidontheweb.inria.fr associated with source document(s)

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hasSource	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. In vitro 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.
hasSelector	covid:ann/selector/cdd27de1e887a76615a1be0e0bf6e02a6da7e182
is hasTarget of	named entity 'KNOCK-OUT'

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