Characterization of glycoprotein E C-End of West Nile virus and evaluation of its interaction force with aVb3 integrin as putative cellular receptor

• Published in: Biochemistry (Moscow) Vol. 75; no. 4; pp. 472 - 480
• Main Authors: Bogachek, M V, Zaitsev, B N, Sekatskii, S K, Protopopova, E V, Ternovoi, V A, Ivanova, A V, Kachko, A V, Ivanisenko, V A, Dietler, G, Loktev, V B
• Format: Journal Article
• Language: English
• Published: 01-04-2010
• Subjects: West Nile virus
• ISSN: 0006-2979; 1608-3040
• DOI: 10.1134/S0006297910040115

Recombinant polypeptide containing the 260-466 amino acid sequence of West Nile virus (WNV) strain LEIV-Vlg99-27889-human glycoprotein E (gpE, E sub(260-466)) was constructed. Immunochemical similarity between the E sub(260-466) and gpE of WNV was proven by enzyme immunoassay (EIA), immunoblot, competitive EIA, hemagglutination inhibition, and neutralization tests using polyclonal and monoclonal antibodies against the viral gpE and recombinant E sub(260-466). Polypeptide E sub(260-466) induced formation of virus neutralizing and cross-reactive antibodies that were interactive with various epitopes of this recombinant protein. It is shown by evaluation of the interaction of E sub(260-466) with one of the proposed cell receptors of WNV that average E sub(260-466)-aVb3 integrin-specific interaction force measured using atomic force spectroscopy was 80 and 140 pN for single and double interactions, correspondingly. Taken together with previously described interaction between laminin-binding protein (LBP) and WNV gpE domain II, it is proposed that WNV gpE can interact specifically with two cellular proteins (LBP and aVb3 integrin) during virus entry.