3M5H

Crystal structure of a H7 influenza virus hemagglutinin complexed with 3SLN

Summary for 3M5H

• Entry DOI: 10.2210/pdb3m5h/pdb
• Related: 3M5G 3M5I 3M5J
• 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, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: influenza virus, hemagglutinin, 3sln, envelope protein, fusion protein, host cell membrane, host membrane, membrane, transmembrane, virion, viral protein
• Biological source: Influenza A virus; More
• Total number of polymer chains: 6
• Total formula weight: 171251.65

Authors

Yang, H.,Chen, L.M.,Carney, P.J.,Donis, R.O.,Stevens, J. (deposition date: 2010-03-12, release date: 2010-09-22, Last modification date: 2024-11-06)

Primary citation

Yang, H.,Chen, L.M.,Carney, P.J.,Donis, R.O.,Stevens, J.
Structures of receptor complexes of a North American H7N2 influenza hemagglutinin with a loop deletion in the receptor binding site.
Plos Pathog., 6:e1001081-e1001081, 2010

PubMed Abstract: Human infections with subtype H7 avian influenza viruses have been reported as early as 1979. In 1996, a genetically stable 24-nucleotide deletion emerged in North American H7 influenza virus hemagglutinins, resulting in an eight amino acid deletion in the receptor-binding site. The continuous circulation of these viruses in live bird markets, as well as its documented ability to infect humans, raises the question of how these viruses achieve structural stability and functionality. Here we report a detailed molecular analysis of the receptor binding site of the North American lineage subtype H7N2 virus A/New York/107/2003 (NY107), including complexes with an avian receptor analog (3'-sialyl-N-acetyllactosamine, 3'SLN) and two human receptor analogs (6'-sialyl-N-acetyllactosamine, 6'SLN; sialyllacto-N-tetraose b, LSTb). Structural results suggest a novel mechanism by which residues Arg220 and Arg229 (H3 numbering) are used to compensate for the deletion of the 220-loop and form interactions with the receptor analogs. Glycan microarray results reveal that NY107 maintains an avian-type (alpha2-3) receptor binding profile, with only moderate binding to human-type (alpha2-6) receptor. Thus despite its dramatically altered receptor binding site, this HA maintains functionality and confirms a need for continued influenza virus surveillance of avian and other animal reservoirs to define their zoonotic potential.

PubMed: 20824086
DOI: 10.1371/journal.ppat.1001081

Experimental method

X-RAY DIFFRACTION (2.7 Å)