N-Glycolylneuraminic Acid as a Receptor for Influenza A Viruses

被引:76
作者
Broszeit, Frederik [1 ]
Tzarum, Netanel [2 ]
Zhu, Xueyong [2 ]
Nemanichvili, Nikoloz [3 ]
Eggink, Dirk [4 ]
Leenders, Tim [1 ]
Li, Zeshi [1 ]
Liu, Lin [5 ]
Wolfert, Margreet A. [1 ,5 ]
Papanikolaou, Andreas [3 ]
Martinez-Romero, Caries [6 ,7 ]
Gagarinov, Ivan A. [1 ]
Yu, Wenli [2 ]
Garcia-Sastre, Adolfo [6 ,7 ,8 ]
Wennekes, Tom [1 ]
Okamatsu, Masatoshi [9 ]
Verheije, Monique H. [3 ]
Wilson, Ian A. [2 ,10 ]
Boons, Geert-Jan [1 ,5 ]
de Vries, Robert P. [1 ]
机构
[1] Univ Utrecht, Utrecht Inst Pharmaceut Sci, Dept Chem Biol & Drug Discovery, NL-3584 CG Utrecht, Netherlands
[2] Scripps Res Inst, Dept Integrat Struct & Computat Biol, La Jolla, CA 92037 USA
[3] Univ Utrecht, Fac Vet Med, Dept Pathobiol, NL-3584 CL Utrecht, Netherlands
[4] Amsterdam Med Ctr, Dept Expt Virol, Amsterdam, Netherlands
[5] Univ Georgia, Complex Carbohydrate Res Ctr, Athens, GA 30602 USA
[6] Icahn Sch Med Mt Sinai, Dept Microbiol, New York, NY 10029 USA
[7] Icahn Sch Med Mt Sinai, Global Hlth & Emerging Pathogens Inst, New York, NY 10029 USA
[8] Icahn Sch Med Mt Sinai, Dept Med, Div Infect Dis, New York, NY 10029 USA
[9] Hokkaido Univ, Grad Sch Vet Med, Dept Dis Control, Lab Microbiol, Sapporo, Hokkaido, Japan
[10] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
关键词
SIALIC ACIDS; ENZYMATIC-ACTIVITY; SCALE PRODUCTION; SPECIFICITY; BINDING; HEMAGGLUTININ; NEURAMINIDASE; RECOGNITION; SIALYLGLYCOPEPTIDE; EXPRESSION;
D O I
10.1016/j.celrep.2019.05.048
中图分类号
Q2 [细胞生物学];
学科分类号
071013 [干细胞生物学];
摘要
A species barrier for the influenza A virus is the differential expression of sialic acid, which can either be alpha 2,3-linked for avians or alpha 2,6-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 alpha 2,3- and alpha 2,6-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.
引用
收藏
页码:3284 / +
页数:17
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