4N60

Crystal structure of hemagglutinin from an H7N9 influenza virus in complex with LSTc

Summary for 4N60

• Entry DOI: 10.2210/pdb4n60/pdb
• Related: 4N5J 4N5K
• Descriptor: Hemagglutinin HA1, Hemagglutinin HA2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• Functional Keywords: viral envelope protein, hemagglutinin, viral fusion protein, viral protein
• Biological source: Influenza A virus; More
• Total number of polymer chains: 4
• Total formula weight: 113272.32

Authors

Xu, R.,Wilson, I.A. (deposition date: 2013-10-11, release date: 2013-12-18, Last modification date: 2024-10-30)

Primary citation

Xu, R.,de Vries, R.P.,Zhu, X.,Nycholat, C.M.,McBride, R.,Yu, W.,Paulson, J.C.,Wilson, I.A.
Preferential recognition of avian-like receptors in human influenza A H7N9 viruses.
Science, 342:1230-1235, 2013

PubMed Abstract: The 2013 outbreak of avian-origin H7N9 influenza in eastern China has raised concerns about its ability to transmit in the human population. The hemagglutinin glycoprotein of most human H7N9 viruses carries Leu(226), a residue linked to adaptation of H2N2 and H3N2 pandemic viruses to human receptors. However, glycan array analysis of the H7 hemagglutinin reveals negligible binding to humanlike α2-6-linked receptors and strong preference for a subset of avian-like α2-3-linked glycans recognized by all avian H7 viruses. Crystal structures of H7N9 hemagglutinin and six hemagglutinin-glycan complexes have elucidated the structural basis for preferential recognition of avian-like receptors. These findings suggest that the current human H7N9 viruses are poorly adapted for efficient human-to-human transmission.

PubMed: 24311689
DOI: 10.1126/science.1243761

Experimental method

X-RAY DIFFRACTION (2.9032 Å)