9DIO

Crystal structure of H5 hemagglutinin Q226L mutant from the influenza virus A/Texas/37/2024 (H5N1) with LSTc

Summary for 9DIO

• Entry DOI: 10.2210/pdb9dio/pdb
• Related PRD ID: PRD_900046
• Descriptor: Hemagglutinin HA1, Hemagglutinin HA2, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose, ... (10 entities in total)
• Functional Keywords: h1n1, antibody, hemagglutinin, viral protein
• Biological source: Influenza A virus; More
• Total number of polymer chains: 18
• Total formula weight: 524089.66

Authors

Lin, T.H.,Zhu, Y.,Wilson, I.A. (deposition date: 2024-09-05, release date: 2024-12-04, Last modification date: 2025-01-22)

Primary citation

Lin, T.H.,Zhu, X.,Wang, S.,Zhang, D.,McBride, R.,Yu, W.,Babarinde, S.,Paulson, J.C.,Wilson, I.A.
A single mutation in bovine influenza H5N1 hemagglutinin switches specificity to human receptors.
Science, 386:1128-1134, 2024

PubMed Abstract: 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 GlnLeu substitution switched Texas HA binding specificity to human-type receptors, which was enhanced when combined with an AsnLys mutation. Crystal structures of the Texas HA with avian receptor analog LSTa and its GlnLeu 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.

PubMed: 39636969
DOI: 10.1126/science.adt0180

Experimental method

X-RAY DIFFRACTION (2.7 Å)