PDBsum entry 5e34

Viral protein

PDB id: 5e34

Contents

Protein chains

323 a.a.

175 a.a.

Ligands

NAG-GAL-SIA

NAG ×2

Waters ×90

PDB id:

5e34

Name:

Viral protein

Title:

Crystal structure of h5 hemagglutinin mutant (n224k, q226l, n158d and l133a deletion) from the influenza virus a/chicken/vietnam/ncvd- 093/2008 (h5n1) with lsta

Structure:

Hemagglutinin. Chain: a. Fragment: unp residues 17-346. Synonym: hemagglutinin ha1 chain. Engineered: yes. Mutation: yes. Hemagglutinin. Chain: b. Fragment: unp residues 347-521.

Source:

Influenza a virus (a/chicken/vietnam/ncvd- 093/2008(h5n1)). Organism_taxid: 581024. Strain: a/chicken/vietnam/ncvd-093/2008(h5n1). Gene: ha. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Influenza a virus.

Resolution:

2.70Å R-factor: 0.216 R-free: 0.250

Authors:

X.Zhu,I.A.Wilson

Key ref:

X.Zhu et al. (2015). Structural Basis for a Switch in Receptor Binding Specificity of Two H5N1 Hemagglutinin Mutants. Cell Rep, 13, 1683-1691. PubMed id: 26586437 DOI: 10.1016/j.celrep.2015.10.027

Date:

01-Oct-15 Release date: 02-Dec-15

Protein chain

C4P282  (C4P282_9INFA) -  Hemagglutinin from Influenza A virus

Seq: 568 a.a.

Struc: 323 a.a.*

Protein chain

C4P282  (C4P282_9INFA) -  Hemagglutinin from Influenza A virus

Seq: 568 a.a.

Struc: 175 a.a.

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1016/j.celrep.2015.10.027

Cell Rep 13:1683-1691 (2015)

PubMed id: 26586437

Structural Basis for a Switch in Receptor Binding Specificity of Two H5N1 Hemagglutinin Mutants.

X.Zhu, K.Viswanathan, R.Raman, W.Yu, R.Sasisekharan, I.A.Wilson.

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 α2-6-linked sialosides with avidity comparable to wild-type H5 HA binding to avian-like α2-3-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.