TY - JOUR
T1 - N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses
AU - Broszeit, Frederik
AU - Tzarum, Netanel
AU - Zhu, Xueyong
AU - Nemanichvili, Nikoloz
AU - Eggink, Dirk
AU - Leenders, Tim
AU - Li, Zeshi
AU - Liu, Lin
AU - Wolfert, Margreet A.
AU - Papanikolaou, Andreas
AU - Martínez-Romero, Carles
AU - Gagarinov, Ivan A.
AU - Yu, Wenli
AU - García-Sastre, Adolfo
AU - Wennekes, Tom
AU - Okamatsu, Masatoshi
AU - Verheije, Monique H.
AU - Wilson, Ian A.
AU - Boons, Geert-Jan
AU - de Vries, Robert P.
PY - 2019
Y1 - 2019
N2 - 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.
AB - 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.
UR - https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85066307306&origin=inward
UR - https://www.ncbi.nlm.nih.gov/pubmed/31189111
U2 - https://doi.org/10.1016/j.celrep.2019.05.048
DO - https://doi.org/10.1016/j.celrep.2019.05.048
M3 - Article
C2 - 31189111
SN - 2211-1247
VL - 27
SP - 3284-3294.e6
JO - Cell reports
JF - Cell reports
IS - 11
ER -