Generation and characterisation of monoclonal antibodies specific to avian influenza H7N9 haemagglutinin protein

• Published in: Indian journal of medical microbiology Vol. 34; no. 4; pp. 489 - 494
• Main Authors: Malik, A, Mallajosyula, VVA, Mishra, NN, Arukha, AP, Varadarajan, R, Gupta, SK
• Format: Journal Article
• Language: English
• Published: India Elsevier B.V 01.10.2016; Wolters Kluwer India Pvt. Ltd; Elsevier Limited
• Subjects: Animals; Antibodies, Monoclonal - isolation & purification; Antibodies, Viral - isolation & purification; Avian influenza; Blotting, Western; Enzyme-Linked Immunosorbent Assay; Female; H7N9; Hemagglutinin Glycoproteins, Influenza Virus - genetics; Hemagglutinin Glycoproteins, Influenza Virus - immunology; Influenza A Virus, H7N9 Subtype - genetics; Influenza A Virus, H7N9 Subtype - immunology; Mice, Inbred BALB C; monoclonal antibodies; Orthomyxoviridae; Recombinant Proteins - genetics; Recombinant Proteins - immunology; Avian influenza; H7N9; monoclonal antibodies
• ISSN: 0255-0857; 1998-3646
• DOI: 10.4103/0255-0857.195366

Introduction: Emerging virulent strains of influenza virus pose a serious public health threat with potential pandemic consequences. A novel avian influenza virus, H7N9, breached the species barrier from infected domestic poultry to humans in 2013 in China. Since then, it has caused numerous infections in humans with a close contact to poultry. Materials and Methods: In this study, we describe the preliminary characterisation of five murine monoclonal antibodies (MAbs) developed against recombinant haemagglutinin (rHA) protein of avian H7N9 A/Anhui/1/2013 virus by their Western blot and enzyme-linked immunosorbent assay (ELISA) reactivity and binding affinity. Results: Of the five MAbs, four were highly specific to H7N9 HA and did not show any cross-reactivity in ELISA with rHA protein from pandemic as well as seasonal H1N1, H2N2, H3N2, H5N1 and influenza virus B (B/Brisbane/60/2008). However, one of the MAbs, MA-24, in addition to HA protein of H7N9 also reacted strongly with HA protein of H3N2 and weakly with HA of pandemic and seasonal H1N1 and H2N2. All the five MAbs also reacted with H7N9 rHA in Western blot. The MAbs bound H7N9 rHA with an equilibrium dissociation constant (KD) ranging between 0.14 and 25.20 nM, indicating their high affinity to HA. Conclusions: These antibodies may be useful in developing diagnostic tools for the detection of influenza H7N9 virus infections.