학술논문

Recombinant hemagglutinin glycoproteins provide insight into binding to host cells by H5 influenza viruses in wild and domestic birds.
Document Type
article
Source
Subject
Intestinal Mucosa
Lung
Bursa of Fabricius
Cloaca
Animals
Animals
Domestic
Animals
Wild
Ducks
Eagles
Poultry
Recombinant Proteins
Hemagglutinin Glycoproteins
Influenza Virus
Virulence
Gene Expression
Protein Binding
Influenza in Birds
Influenza A Virus
H5N2 Subtype
Viral Tropism
H5N2
Hemagglutinin
Highly pathogenic avian influenza virus
Low pathogenic avian influenza virus
Recombinant protein
Terrestrial birds
Tropism
Waterfowl
Influenza
Infectious Diseases
Emerging Infectious Diseases
Biodefense
Pneumonia & Influenza
Vaccine Related
Prevention
Aetiology
2.2 Factors relating to the physical environment
Infection
Biological Sciences
Agricultural and Veterinary Sciences
Medical and Health Sciences
Virology
Language
Abstract
Clade 2.3.4.4, H5 subtype highly pathogenic avian influenza viruses (HPAIVs) have caused devastating effects across wild and domestic bird populations. We investigated differences in the intensity and distribution of the hemagglutinin (HA) glycoprotein binding of a clade 2.3.4.4 H5 HPAIV compared to a H5 low pathogenic avian influenza virus (LPAIV). Recombinant HA from gene sequences from a HPAIV, A/Northern pintail/Washington/40964/2014(H5N2) and a LPAIV, A/mallard/MN/410/2000(H5N2) were generated and, via protein histochemistry, HA binding in respiratory, intestinal and cloacal bursal tissue was quantified as median area of binding (MAB). Poultry species, shorebirds, ducks and terrestrial birds were used. Differences in MAB were observed between the HPAIV and LPAIV H5 HAs. We demonstrate that clade 2.3.4.4 HPAIV H5 HA has a broader host cell binding across a variety of bird species compared to the LPAIV H5 HA. These findings support published results from experimental trials, and outcomes of natural disease outbreaks with these viruses.