The index influenza A virus subtype H5N1 isolated from a human in 1997 differs in its receptor-binding properties from a virulent avian influenza virus.

Kiyoko Iwatsuki-Horimoto1,2 Rie Kanazawa3 Shunji Sugii3 Yoshihiro Kawaoka4,1,2 Taisuke Horimoto1,2
Affiliations 4 institutions
  1. Core Research for Evolutional Science and Technology (CREST), Japan Science and Technology Corporation, Saitama 332-0012, Japan.
  2. Division of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Tokyo 108-8639, Japan.
  3. Laboratory of Veterinary Microbiology, Division of Veterinary Science, Graduate School of Agriculture and Biological Sciences, Osaka Prefecture University, 1-1 Gakuen-cho, Sakai, Osaka 599-8531, Japan.
  4. Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin, Madison, WI 53706, USA.

Abstract

To gain insight into the events that occur when avian influenza viruses are transmitted to humans, the receptor-binding properties of the index H5N1 influenza virus isolated from a human in 1997 and the A/turkey/Ontario/7732/66 (H5N9) virus were compared, by using a haemadsorption assay. Cells expressing the haemagglutinin (HA) of the human isolate were adsorbed by both chicken red blood cells (RBCs) and human RBCs; those expressing the avian virus HA were only adsorbed by chicken RBCs. These results indicate that human and avian influenza virus H5 HAs differ in their recognition of sialyloligosaccharides on the RBCs of different animal species. Mutational analyses indicated that differences in both the oligosaccharide chains and in the amino acid sequences around the HA receptor-binding site were responsible for this difference in receptor binding. These data further support the concept that alteration in receptor recognition is important for replication of avian viruses in humans.

Supporting text Virus Host Location
Influenza A Virus, H5N1 Subtype 300 Animals 1948 Chickens 146 Hemagglutinins, Viral 12 Humans 1440 In Vitro Techniques 5 Influenza A virus 186 Models, Molecular 99 Mutagenesis, Site-Directed 12 Protein Conformation 44 Receptors, Virus 204 Virulence 108 Virus Replication 191

Evidence records

1 total
Functional Mechanism
1 records · 1 evidence types
Evidence type
1 records
OVE160
Key finding

The HA of the human H5N1 influenza virus binds both chicken and human red blood cells, indicating broader receptor recognition than the avian H5N9 HA which binds only chicken RBCs.

Virus
Host
Location
Not specified
Supporting text

Cells expressing the haemagglutinin (HA) of the human isolate were adsorbed by both chicken red blood cells (RBCs) and human RBCs; those expressing the avian virus HA were only adsorbed by chicken RBCs.

Method
haemadsorption assay | mutational analysis
Receptors
sialyloligosaccharides