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10.1099/jgv.0.001408 http://scihub22266oqcxt.onion/10.1099/jgv.0.001408 32213247!7414442!32213247     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Gen+Virol 2020 ; 101 (6): 599-608 Nephropedia Template TP {{tp|p=32213247|t=2020. N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity |pdf=|usr=}}{{32213247}} gab.com Text N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity JO: J Gen Virol http://www.kidney.de/pget.php?&tw=1&pmid=32213247 #FOAvip 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. Twit Text FOAVip N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity ????J Gen Virol http://www.kidney.de/pget.php?&tw=1&pmid=32213247 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32213247 #FOAvip English Wikipedia <ref>{{Cite pmid|32213247}}</ref> N-glycosylation of infectious bronchitis virus M41 spike determines receptor specificity #MMPMID32213247 Bouwman KM; Habraeken N; Laconi A; Berends AJ; Groenewoud L; Alders M; Kemp V; Verheije MH J Gen Virol 2020[Jun]; 101 (6): 599-608 PMID32213247show ga 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. |*Protein Domains[MESH] |Animals[MESH] |Cell Line[MESH] |Chick Embryo[MESH] |Coronavirus Infections/*immunology/virology[MESH] |Glycosylation[MESH] |Host Specificity/*immunology[MESH] |Infectious bronchitis virus/*chemistry/immunology[MESH] |Kidney/cytology/embryology[MESH] |Protein Binding[MESH] |Receptors, Cell Surface/metabolism[MESH] |Receptors, Virus/*immunology/metabolism[MESH] |Recombinant Proteins[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/metabolism[MESH] |Viral Tropism/immunology[MESH] |Virus Attachment[MESH]N-glycosylation of infectious bronchitis virus M41 spike determines re(epmc).pdf DeepDyve Pubget Overpricing