4K63

Structure of an avian influenza H5 hemagglutinin from the influenza virus complexed with avian receptor analog LSTa

Summary for 4K63

• Entry DOI: 10.2210/pdb4k63/pdb
• Related: 4K62 4K64 4K65 4K66 4K67
• Related PRD ID: PRD_900067
• Descriptor: Hemagglutinin, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose, ... (5 entities in total)
• Functional Keywords: virus attachment, membrane fusion, viral protein
• Biological source: Influenza A virus; More
• Total number of polymer chains: 8
• Total formula weight: 223356.57

Authors

Zhang, W.,Shi, Y.,Lu, X.,Shu, Y.,Qi, J.,Gao, G.F. (deposition date: 2013-04-15, release date: 2013-05-22, Last modification date: 2024-10-30)

Primary citation

Zhang, W.,Shi, Y.,Lu, X.,Shu, Y.,Qi, J.,Gao, G.F.
An airborne transmissible avian influenza H5 hemagglutinin seen at the atomic level.
Science, 340:1463-1467, 2013

PubMed Abstract: Recent studies have identified several mutations in the hemagglutinin (HA) protein that allow the highly pathogenic avian H5N1 influenza A virus to transmit between mammals by airborne route. Here, we determined the complex structures of wild-type and mutant HAs derived from an Indonesia H5N1 virus bound to either avian or human receptor sialic acid analogs. A cis/trans conformational change in the glycosidic linkage of the receptor analog was observed, which explains how the H5N1 virus alters its receptor-binding preference. Furthermore, the mutant HA possessed low affinities for both avian and human receptors. Our findings provide a structural and biophysical basis for the H5N1 adaptation to acquire human, but maintain avian, receptor-binding properties.

PubMed: 23641058
DOI: 10.1126/science.1236787

Experimental method

X-RAY DIFFRACTION (3.1 Å)