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N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses.

Authors :
Broszeit F
Tzarum N
Zhu X
Nemanichvili N
Eggink D
Leenders T
Li Z
Liu L
Wolfert MA
Papanikolaou A
Martínez-Romero C
Gagarinov IA
Yu W
García-Sastre A
Wennekes T
Okamatsu M
Verheije MH
Wilson IA
Boons GJ
de Vries RP
Source :
Cell reports [Cell Rep] 2019 Jun 11; Vol. 27 (11), pp. 3284-3294.e6.
Publication Year :
2019

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.<br /> (Copyright © 2019 The Authors. Published by Elsevier Inc. All rights reserved.)

Details

Language :
English
ISSN :
2211-1247
Volume :
27
Issue :
11
Database :
MEDLINE
Journal :
Cell reports
Publication Type :
Academic Journal
Accession number :
31189111
Full Text :
https://doi.org/10.1016/j.celrep.2019.05.048