Universal anti-neuraminidase antibody inhibiting all influenza A subtypes
| Autor: | Gary Van Domselaar, Louise Larocque, Junzhi Wang, Earl G. Brown, Aaron Farnsworth, Changgui Li, Terry D. Cyr, Tracey M. Doyle, Aeron C. Hurt, Anwar M. Hashem, Xuguang Li, Daryl G.S. Smith, Runtao He |
|---|---|
| Rok vydání: | 2013 |
| Předmět: |
medicine.drug_class
viruses Cross Protection Neuraminidase Monoclonal antibody Antibodies Viral Epitope Conserved sequence Mice Viral Proteins Influenza A Virus H1N1 Subtype Orthomyxoviridae Infections Virology Viral neuraminidase medicine Animals Pharmacology chemistry.chemical_classification biology Influenza A Virus H3N2 Subtype Antibodies Monoclonal Amino acid Disease Models Animal chemistry Viral replication biology.protein Epitopes B-Lymphocyte Female Antibody |
| Zdroj: | Antiviral research. 100(2) |
| ISSN: | 1872-9096 |
| Popis: | The only universally conserved sequence amongst all influenza A viral neuraminidase (NA) is located between amino acids 222-230 and plays crucial roles in viral replication. However, it remained unclear as to whether this universal epitope is exposed during the course of infection to allow binding and inhibition by antibodies. Using a monoclonal antibody (MAb) targeting this specific epitope, we demonstrated that all nine subtypes of NA were inhibited in vitro by the MAb. Moreover, the antibody also provided heterosubtypic protection in mice challenged with lethal doses of mouse-adapted H1N1 and H3N2, which represent group I and II viruses, respectively. Furthermore, we report amino acid residues I222 and E227, located in close proximity to the active site, are indispensable for inhibition by this antibody. This unique, highly-conserved linear sequence in viral NA could be an attractive immunological target for protection against diverse strains of influenza viruses. |
| Databáze: | OpenAIRE |
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