5E30: Crystal Structure Of H5 Hemagglutinin Q226l Mutant From The Influenza Virus A/duck/egypt/10185ss/2010 (h5n1) With Lstc

Citation:
Abstract
Avian H5N1 influenza viruses continue to spread in wild birds and domestic poultry with sporadic infection in humans. Receptor binding specificity changes are a prerequisite for H5N1 viruses and other zoonotic viruses to be transmitted among humans. Previous reported hemagglutinin (HA) mutants from ferret-transmissible H5N1 viruses of A/Vietnam/1203/2004 and A/Indonesia/5/2005 showed slightly increased, but still very weak, binding to human receptors. From mutagenesis and glycan array studies, we previously identified two H5N1 HA mutants that could more effectively switch receptor specificity to human-like alpha2-6-linked sialosides with avidity comparable to wild-type H5 HA binding to avian-like alpha2-3-linked sialosides. Here, crystal structures of these two H5 HA mutants free and in complex with human and avian glycan receptor analogs reveal the structural basis for their preferential binding to human receptors. These findings suggest continuous surveillance should be maintained to monitor and assess human-to-human transmission potential of H5N1 viruses.
PDB ID: 5E30Download
MMDB ID: 134581
PDB Deposition Date: 2015/10/1
Updated in MMDB: 2015/12
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 5E30: hexameric; determined by author and by software (PISA)
Molecular Components in 5E30
Label Count Molecule
Proteins (6 molecules)
3
Hemagglutinin
Molecule annotation
3
Hemagglutinin
Molecule annotation
Chemicals (24 molecules)
1
11
2
1
3
3
4
3
5
6
* Click molecule labels to explore molecular sequence information.

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