Evol Bioinform Online. 2019 Sep 16;15:1176934319876938. doi: 10.1177/1176934319876938. eCollection 2019.
Molecular Docking of Broad-Spectrum Antibodies on Hemagglutinins of Influenza A Virus.

Le KP1, Do PC1, Amaro RE2, Le L1,2.
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1 School of Biotechnology, International University, Vietnam National University, Ho Chi Minh City, Vietnam. 2 Department of Chemistry and Biochemistry, University of California, San Diego, CA, USA.


Influenza A has caused several deadly pandemics throughout human history. The virus is often resistant to developed treatments because of its genetic drift or shift property. Broad-spectrum antibodies show a promising potential to overcome the resistance of influenza viruses. In silico studies on broad-reactive antibodies and their interactions with hemagglutinins might shed light on the rational design of a universal vaccine. In this study, 11 broad-spectrum antibodies (or antigen-binding fragments) and 14 hemagglutinins of H3N2 and H5N1 strains were docked and analyzed to provide information about the construction of the scaffold for using universal antibodies against the influenza A virus. Antigen-binding fragments that have high number of appearances in the top 3 within each H3 and H5 subtypes were chosen for protein-protein interaction analysis. The results show that while the hydrogen bond is important for Ab/Fab binding to H3, the H5-Ab/Fab system may need cation-pi interaction for a strong interaction.


Hemagglutinin; MEGADOCK; broad-spectrum antibody; protein-protein interaction; universal vaccine

PMID: 31555044 PMCID: PMC6747855 DOI: 10.1177/1176934319876938