血凝素(流感)
H5N1亚型流感病毒
病毒学
受体
突变体
生物
克莱德
突变
病毒
遗传学
基因
系统发育树
作者
Ting-Hui Lin,Xueyong Zhu,Shengyang Wang,Ding Zhang,Ryan McBride,Wenli Yu,Simeon Babarinde,James C. Paulson,Ian A. Wilson
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2024-12-05
卷期号:386 (6726): 1128-1134
标识
DOI:10.1126/science.adt0180
摘要
In 2024, several human infections with highly pathogenic clade 2.3.4.4b bovine influenza H5N1 viruses in the United States raised concerns about their capability for bovine-to-human or even human-to-human transmission. In this study, analysis of the hemagglutinin (HA) from the first-reported human-infecting bovine H5N1 virus (A/Texas/37/2024, Texas) revealed avian-type receptor binding preference. Notably, a Gln 226 Leu substitution switched Texas HA binding specificity to human-type receptors, which was enhanced when combined with an Asn 224 Lys mutation. Crystal structures of the Texas HA with avian receptor analog LSTa and its Gln 226 Leu mutant with human receptor analog LSTc elucidated the structural basis for this preferential receptor recognition. These findings highlight the need for continuous surveillance of emerging mutations in avian and bovine clade 2.3.4.4b H5N1 viruses.
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