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Publication Abstract from PubMed

A species barrier for the influenza A virus is the differential expression of sialic acid, which can either be alpha2,3-linked for avians or alpha2,6-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 alpha2,3- and alpha2,6-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.

N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses.,Broszeit F, Tzarum N, Zhu X, Nemanichvili N, Eggink D, Leenders T, Li Z, Liu L, Wolfert MA, Papanikolaou A, Martinez-Romero C, Gagarinov IA, Yu W, Garcia-Sastre A, Wennekes T, Okamatsu M, Verheije MH, Wilson IA, Boons GJ, de Vries RP Cell Rep. 2019 Jun 11;27(11):3284-3294.e6. doi: 10.1016/j.celrep.2019.05.048. PMID:31189111^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.