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Literature detail

Structural and functional analysis of surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals.

Hua Yang1 Ha T Nguyen2 Paul J Carney1 Zhu Guo1 Jessie C Chang1 Joyce Jones1 Charles T Davis1 Julie M Villanueva1 Larisa V Gubareva1 James Stevens3
Affiliations 3 institutions
  1. Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia, USA.
  2. Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia, USA Battelle Memorial Institute, Atlanta, Georgia, USA.
  3. Influenza Division, National Center for Immunization and Respiratory Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia, USA [email protected].
PMID 25540377 2015 J Virol eng ppublish
PubMed DOI Browse context

Article

Publication summary

In late 2011, an A(H3N8) influenza virus infection resulted in the deaths of 162 New England harbor seals. Virus sequence analysis and virus receptor binding studies highlighted potential markers responsible for mammalian adaptation and a mixed receptor binding preference (S. J. Anthony, J. A. St Leger, K. Pugliares, H. S. Ip, J. M. Chan, Z. W. Carpenter, I. Navarrete-Macias, M. Sanchez-Leon, J. T. Saliki, J. Pedersen, W. Karesh, P. Daszak, R. Rabadan, T. Rowles, W. I. Lipkin, MBio 3:e00166-00112, 2012, http://dx.doi.org/10.1128/mBio.00166-12). Here, we present a detailed structural and biochemical analysis of the surface antigens of the virus. Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase indicate a true avian receptor binding preference. Although the detection of this virus in new species highlights an increased potential for cross-species transmission, our results indicate that the A(H3N8) virus currently poses a low risk to humans. Cross-species transmission of zoonotic influenza viruses increases public health concerns. Here, we report a molecular and structural study of the major surface proteins from an A(H3N8) influenza virus isolated from New England harbor seals. The results improve our understanding of these viruses as they evolve and provide important information to aid ongoing risk assessment analyses as these zoonotic influenza viruses continue to circulate and adapt to new hosts.

Virus Attachment Amino Acid Sequence Animals Antigens, Viral Crystallography, X-Ray Hemagglutinin Glycoproteins, Influenza Virus Influenza A Virus, H3N8 Subtype Microbial Sensitivity Tests Models, Molecular Molecular Sequence Data Neuraminidase New England Orthomyxoviridae Infections Phoca Polysaccharides Protein Binding Protein Conformation Recombinant Proteins

Structured evidence records

Evidence records

4 total
Cross Species Transmission 1 records
Cross Species Transmission Extraction confidence 0.95
Key finding

An avian-lineage A(H3N8) influenza virus was detected in harbor seals, demonstrating cross-species transmission between birds and marine mammals.

Virus
IAV H3N8
Location
United States New England, United States
Supporting text

Although the detection of this virus in new species highlights an increased potential for cross-species transmission, our results indicate that the A(H3N8) virus currently poses a low risk to humans.

Method
virus sequence analysis; receptor binding studies; structural and biochemical analysis
Study design
molecular and structural analysis
Transmission direction
animal-to-animal
Geographic raw
New England
Country inferred
United States
Genomic Evolution 1 records
Genomic Evolution Extraction confidence 0.70
Key finding

Sequence and structural analyses of hemagglutinin and neuraminidase from seal-derived A(H3N8) influenza virus revealed avian-like receptor specificity and molecular features related to mammalian adaptation.

Virus
IAV H3N8
Location
Not specified
Supporting text

Virus sequence analysis and virus receptor binding studies highlighted potential markers responsible for mammalian adaptation and a mixed receptor binding preference. Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase indicate a true avian receptor binding preference.

Genes or proteins
hemagglutinin; neuraminidase
Analysis methods
sequence analysis; structural analysis
Molecular Adaptation 1 records
Molecular Adaptation Extraction confidence 0.90
Key finding

A(H3N8) influenza virus from harbor seals shows structural and functional features in hemagglutinin and neuraminidase consistent with avian receptor binding, indicating limited adaptation to mammalian hosts.

Virus
IAV H3N8
Host
Not specified
Location
Not specified
Supporting text

Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase indicate a true avian receptor binding preference. Virus sequence analysis and receptor binding studies highlighted potential markers responsible for mammalian adaptation.

Genes or proteins
hemagglutinin; neuraminidase
Receptors
avian receptor
Mechanism types
receptor_binding; host_adaptation
Receptor Usage 1 records
Receptor Usage Extraction confidence 0.95
Key finding

The A(H3N8) influenza virus isolated from harbor seals binds preferentially to avian-type receptors based on hemagglutinin and neuraminidase structural analysis.

Virus
IAV H3N8
Location
Not specified
Supporting text

Results obtained with recombinant proteins for both the hemagglutinin and neuraminidase indicate a true avian receptor binding preference.

Method
structural analysis; biochemical analysis; recombinant protein assay
Receptors
avian receptor