PDBsum entry 4xq5

Viral protein

PDB id: 4xq5

Contents

Protein chains

318 a.a.

171 a.a.

Ligands

NAG-NAG ×3

NAG ×2

Waters ×262

PDB id:

4xq5

Name:

Viral protein

Title:

Human-infecting h10n8 influenza virus retains strong preference for avian-type receptors

Structure:

Hemagglutinin ha1 chain. Chain: a, c, e. Fragment: residues 18-336. Engineered: yes. Hemagglutinin ha2 chain. Chain: b, d, f. Fragment: residues 342-514. Engineered: yes

Source:

Influenza a virus. Organism_taxid: 1458555. Strain: a/jiangxi/ipb13/2013(h10n8). Gene: ha. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.

Resolution:

2.59Å R-factor: 0.193 R-free: 0.230

Authors:

N.Tzarum,H.Zhang,X.Zhu,I.A.Wilson

Key ref:

H.Zhang et al. (2015). A human-infecting H10N8 influenza virus retains a strong preference for avian-type receptors. Cell Host Microbe, 17, 377-384. PubMed id: 25766296 DOI: 10.1016/j.chom.2015.02.006

Date:

19-Jan-15 Release date: 01-Apr-15

Protein chains

A0A059T4A1  (A0A059T4A1_9INFA) -  Hemagglutinin from Influenza A virus

Seq: 561 a.a.

Struc: 318 a.a.

Protein chains

A0A059T4A1  (A0A059T4A1_9INFA) -  Hemagglutinin from Influenza A virus

Seq: 561 a.a.

Struc: 171 a.a.

DOI no: 10.1016/j.chom.2015.02.006

Cell Host Microbe 17:377-384 (2015)

PubMed id: 25766296

A human-infecting H10N8 influenza virus retains a strong preference for avian-type receptors.

H.Zhang, R.P.de Vries, N.Tzarum, X.Zhu, W.Yu, R.McBride, J.C.Paulson, I.A.Wilson.

ABSTRACT

Recent avian-origin H10N8 influenza A viruses that have infected humans pose a potential pandemic threat. Alterations in the viral surface glycoprotein, hemagglutinin (HA), typically are required for influenza A viruses to cross the species barrier for adaptation to a new host, but whether H10N8 contains adaptations supporting human infection remains incompletely understood. We investigated whether H10N8 HA can bind human receptors. Sialoside glycan microarray analysis showed that the H10 HA retains a strong preference for avian receptor analogs and negligible binding to human receptor analogs. Crystal structures of H10 HA with avian and human receptor analogs revealed the basis for preferential recognition of avian-like receptors. Furthermore, introduction of mutations into the H10 receptor-binding site (RBS) known to convert other HA subtypes from avian to human receptor specificity failed to switch preference to human receptors. Collectively, these findings suggest that the current H10N8 human isolates are poorly adapted for efficient human-to-human transmission.