Proteomics

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Glycoengineering of hCK and MDCK for influenza A virus propagation

ABSTRACT: Recent human H3N2 influenza A viruses have evolved to bind elongated glycans terminated with α2,6-linked sialic acids. These extended glycans are of low abundance on cells that are used for the propagation of these viruses, which may explain why it is very difficult to isolate and propagate human H3N2 viruses. This greatly hampers the further study of these viruses. Therefore, we elongated the glycans on cells (MDCK and hCK) by overexpression of the glycosyltransferases that are responsible for building N-acetyllactosamine (LacNAc) repeats, namely B3GNT2 and B4GALT1. Overexpression was clearly shown by qPCR and MS experiments.

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Canis Familiaris (dog) (canis Lupus Familiaris)

SUBMITTER: Joost Snijder  

LAB HEAD: Joost Snijder

PROVIDER: PXD037175 | Pride | 2024-01-26

REPOSITORIES: pride

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Publications

Contemporary human H3N2 influenza A viruses require a low threshold of suitable glycan receptors for efficient infection.

Spruit Cindy M CM   Sweet Igor R IR   Maliepaard Joshua C L JCL   Bestebroer Theo T   Lexmond Pascal P   Qiu Boning B   Damen Mirjam J A MJA   Fouchier Ron A M RAM   Reiding Karli R KR   Snijder Joost J   Herfst Sander S   Boons Geert-Jan GJ   de Vries Robert P RP  

Glycobiology 20231001 10

Recent human H3N2 influenza A viruses have evolved to employ elongated glycans terminating in α2,6-linked sialic acid as their receptors. These glycans are displayed in low abundancies by (humanized) Madin-Darby Canine Kidney cells, which are commonly employed to propagate influenza A virus, resulting in low or no viral propagation. Here, we examined whether the overexpression of the glycosyltransferases β-1,3-N-acetylglucosaminyltransferase and β-1,4-galactosyltransferase 1, which are responsib  ...[more]

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