Characterization of glycoprotein E C-end of West Nile virus and evaluation of its interaction force with alphaVbeta3 integrin as putative cellular receptor

Recombinant polypeptide containing the 260-466 amino acid sequence of West Nile virus (WNV) strain LEIV-Vlg99-27889-human glycoprotein E (gpE, E(260-466)) was constructed. Immunochemical similarity between the E(260-466) and gpE of WNV was proven by enzyme immunoassay (EIA), immunoblot, competitive...

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Published in:Biochemistry (Moscow) 2010-04, Vol.75 (4), p.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: Article
Language:English
Subjects:
Antibodies, Monoclonal - immunology
Antibodies, Neutralizing - immunology
Epitopes - chemistry
Epitopes - immunology
Humans
Integrin alpha5 - chemistry
Integrin alpha5 - metabolism
Microscopy, Atomic Force
Protein Structure, Tertiary
Recombinant Fusion Proteins - chemistry
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Viral Envelope Proteins - chemistry
Viral Envelope Proteins - genetics
Viral Envelope Proteins - metabolism
West Nile virus - metabolism
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Summary:Recombinant polypeptide containing the 260-466 amino acid sequence of West Nile virus (WNV) strain LEIV-Vlg99-27889-human glycoprotein E (gpE, E(260-466)) was constructed. Immunochemical similarity between the E(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(260-466). Polypeptide E(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(260-466) with one of the proposed cell receptors of WNV that average E(260-466)-alphaVbeta3 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 alphaVbeta3 integrin) during virus entry.
ISSN:1608-3040