OmniVira

The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs.

Min Gu1,2 Qunhui Li1 Ruyi Gao1 Dongchang He1 Yunpeng Xu1 Haixu Xu1 Lijun Xu1,3 Xiaoquan Wang1,2 Jiao Hu1,2 Xiaowen Liu1,2 Shunlin Hu1,2 Daxin Peng1,2,4 Xinan Jiao1,2,4 Xiufan Liu5,6,7
Affiliations 7 institutions
  1. College of Veterinary Medicine, Yangzhou University, Yangzhou, Jiangsu, 225009, China.
  2. Jiangsu Key Laboratory of Zoonosis, Yangzhou University, Yangzhou, Jiangsu, 225009, China.
  3. Yangzhou Entry-Exit Inspection and Quarantine Bureau, Yangzhou, Jiangsu, 225009, China.
  4. Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Disease and Zoonoses, Yangzhou, Jiangsu, 225009, China.
  5. College of Veterinary Medicine, Yangzhou University, Yangzhou, Jiangsu, 225009, China. [email protected].
  6. Jiangsu Key Laboratory of Zoonosis, Yangzhou University, Yangzhou, Jiangsu, 225009, China. [email protected].
  7. Jiangsu Co-Innovation Center for the Prevention and Control of Important Animal Infectious Disease and Zoonoses, Yangzhou, Jiangsu, 225009, China. [email protected].
PMID28166830 DOI10.1186/s13567-017-0410-0 Year2017 Journal Veterinary research Vet Res Languageeng Publication statusActive
Active Last checked 2026-10-07 03:30:46 Source: NCBI PubMed

Abstract

We generated and characterized site-directed HA mutants on the genetic backbone of H5N1 clade 2.3.4 virus preferentially binding to α-2,3 receptors in order to identify the key determinants in hemagglutinin rendering the dual affinity to both α-2,3 (avian-type) and α-2,6 (human-type) linked sialic acid receptors of the current clade 2.3.4.4 H5NX subtype avian influenza reassortants. The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only to enhanced binding specificity for human-type receptors but also transmissibility among guinea pigs, which could be considered as an important molecular marker for assessing pandemic potential of H5 subtype avian influenza isolates.

Supporting text Virus Host Location
Amino Acid Substitution 82 Animals 1981 Female 295 Guinea Pigs 21 Hemagglutinin Glycoproteins, Influenza Virus 183 Influenza A Virus, H5N1 Subtype 308 Orthomyxoviridae Infections 235 Receptors, Virus 208 Virus Replication 195

Evidence records

1 total
Functional Mechanism
1 records · 1 evidence types
Evidence type Molecular Adaptation
1 records
OVE2524 Molecular Adaptation
Key finding

The T160A substitution in hemagglutinin of H5N1 clade 2.3.4 avian influenza virus removes glycosylation at 158N, enhancing binding to human-type receptors and increasing transmissibility among guinea pigs.

Virus
Influenza A virus H5N1
Host
Not specified
Location
Not specified
Supporting text

The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only to enhanced binding specificity for human-type receptors but also transmissibility among guinea pigs, which could be considered as an important molecular marker for assessing pandemic potential of H5 subtype avian influenza isolates.

Genes or proteins
hemagglutinin
Receptors
human-type receptors | α-2,6 linked sialic acid receptors
Mutations
T160A
Mechanism types
receptor binding | host-range expansion | transmission fitness