tetano
Editor, Senior Moderator
Cell Rep. 2019 Jun 11;27(11):3284-3294.e6. doi: 10.1016/j.celrep.2019.05.048.
[h=1]N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses.[/h] Broszeit F[SUP]1[/SUP], Tzarum N[SUP]2[/SUP], Zhu X[SUP]2[/SUP], Nemanichvili N[SUP]3[/SUP], Eggink D[SUP]4[/SUP], Leenders T[SUP]1[/SUP], Li Z[SUP]1[/SUP], Liu L[SUP]5[/SUP], Wolfert MA[SUP]6[/SUP], Papanikolaou A[SUP]3[/SUP], Mart?nez-Romero C[SUP]7[/SUP], Gagarinov IA[SUP]1[/SUP], Yu W[SUP]2[/SUP], Garc?a-Sastre A[SUP]8[/SUP], Wennekes T[SUP]1[/SUP], Okamatsu M[SUP]9[/SUP], Verheije MH[SUP]3[/SUP], Wilson IA[SUP]10[/SUP], Boons GJ[SUP]6[/SUP], de Vries RP[SUP]11[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
Copyright ? 2019 The Authors. Published by Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] crystal structure; glycan-array; hemagglutinin; influenza A virus; neuraminidase; receptor-binding; sialic acid
PMID: 31189111 DOI: 10.1016/j.celrep.2019.05.048
[h=1]N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses.[/h] Broszeit F[SUP]1[/SUP], Tzarum N[SUP]2[/SUP], Zhu X[SUP]2[/SUP], Nemanichvili N[SUP]3[/SUP], Eggink D[SUP]4[/SUP], Leenders T[SUP]1[/SUP], Li Z[SUP]1[/SUP], Liu L[SUP]5[/SUP], Wolfert MA[SUP]6[/SUP], Papanikolaou A[SUP]3[/SUP], Mart?nez-Romero C[SUP]7[/SUP], Gagarinov IA[SUP]1[/SUP], Yu W[SUP]2[/SUP], Garc?a-Sastre A[SUP]8[/SUP], Wennekes T[SUP]1[/SUP], Okamatsu M[SUP]9[/SUP], Verheije MH[SUP]3[/SUP], Wilson IA[SUP]10[/SUP], Boons GJ[SUP]6[/SUP], de Vries RP[SUP]11[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] 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.
Copyright ? 2019 The Authors. Published by Elsevier Inc. All rights reserved.
[h=4]KEYWORDS:[/h] crystal structure; glycan-array; hemagglutinin; influenza A virus; neuraminidase; receptor-binding; sialic acid
PMID: 31189111 DOI: 10.1016/j.celrep.2019.05.048