PDBsum entry 5thb

Viral protein

PDB id: 5thb

Contents

Protein chains

318 a.a.

171 a.a.

Ligands

NAG-NAG-BMA-MAN

NAG-NAG

NAG ×5

Waters ×637

PDB id:

5thb

Name:

Viral protein

Title:

Crystal structure of h10 hemagglutinin mutant (t193d-q226l-g228s) from jiangxi-donghu (2013) h10n8 influenza virus

Structure:

Hemagglutinin ha1 chain. Chain: a, c, e. Engineered: yes. Mutation: yes. Hemagglutinin ha2 chain. Chain: b, d, f. Engineered: yes

Source:

Influenza a virus. Organism_taxid: 11320. Strain: jiangxi-donghu (2013) h10n8. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Expression_system_taxid: 7111

Resolution:

2.41Å R-factor: 0.183 R-free: 0.230

Authors:

N.Tzarum,I.A.Wilson

Key ref:

N.Tzarum et al. (2017). The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus. Cell Rep, 19, 235-245. PubMed id: 28402848 DOI: 10.1016/j.celrep.2017.03.054

Date:

29-Sep-16 Release date: 05-Apr-17

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.

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DOI no: 10.1016/j.celrep.2017.03.054

Cell Rep 19:235-245 (2017)

PubMed id: 28402848

The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus.

N.Tzarum, R.P.de Vries, W.Peng, A.J.Thompson, K.M.Bouwman, R.McBride, W.Yu, X.Zhu, M.H.Verheije, J.C.Paulson, I.A.Wilson.

ABSTRACT

Adaptation of influenza A viruses to new hosts are rare events but are the basis for emergence of new influenza pandemics in the human population. Thus, understanding the processes involved in such events is critical for anticipating potential pandemic threats. In 2013, the first case of human infection by an avian H10N8 virus was reported, yet the H10 hemagglutinin (HA) maintains avian receptor specificity. However, the 150-loop of H10 HA, as well as related H7 and H15 subtypes, contains a two-residue insert that can potentially block human receptor binding. Mutation of the 150-loop on the background of Q226L and G228S mutations, which arose in the receptor-binding site of human pandemic H2 and H3 viruses, resulted in acquisition of human-type receptor specificity. Crystal structures of H10 HA mutants with human and avian receptor analogs, receptor-binding studies, and tissue staining experiments illustrate the important role of the 150-loop in H10 receptor specificity.