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N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses

N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses

Frederik Broszeit, Netanel Tzarum, Xueyong Zhu, Nikoloz Nemanichvili, Dirk Eggink, Tim Leenders, Zeshi Li, Lin Liu, Margreet A Wolfert, Andreas Papanikolaou, Carles Martínez-Romero, Ivan A Gagarinov, Wenli Yu, etc.

Cell Rep. 2019 Jun 11;27(11):3284-3294.e6.

PMID: 31189111

Abstract:

A species barrier for the influenza A virus is the differential expression of sialic acid, which can either be α2,3-linked for avians or α2,6-linked for human viruses. The influenza A virus hosts also express other species-specific sialic acid derivatives. One major modification at C-5 is N-glycolyl (NeuGc), instead of N-acetyl (NeuAc). N-glycolyl is mammalian specific and expressed in pigs and horses, but not in humans, ferrets, seals, or dogs. Hemagglutinin (HA) adaptation to either N-acetyl or N-glycolyl is analyzed on a sialoside microarray containing both α2,3- and α2,6-linkage modifications on biologically relevant N-glycans. Binding studies reveal that avian, human, and equine HAs bind either N-glycolyl or N-acetyl. Structural data on N-glycolyl binding HA proteins of both H5 and H7 origin describe this specificity. Neuraminidases can cleave N-glycolyl efficiently, and tissue-binding studies reveal strict species specificity. The exclusive manner in which influenza A viruses differentiate between N-glycolyl and N-acetyl is indicative of selection.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP1113833	N-Glycolylneuraminic acid		1113-83-3	Price

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