Immunochemical and single molecule force spectroscopy studies of specific interaction between the laminin binding protein and the West Nile virus surface glycoprotein E domain II

• Published in: Journal of molecular recognition 2008-01, Vol.21 (1), p.55-62
• Main Authors: Bogachek, Maria V., Protopopova, Elena V., Loktev, Valery B., Zaitsev, Boris N., Favre, Mélanie, Sekatskii, Sergey K., Dietler, Giovanni
• Format: Article
• Language: English
• Subjects: Antibodies, Monoclonal; Biomechanical Phenomena; Blotting, Western; flavivirus surface glycoprotein E; Glycoproteins - chemistry; Glycoproteins - metabolism; Humans; Immunoenzyme Techniques; Immunohistochemistry; laminin binding protein; Microscopy, Atomic Force; Peptides - metabolism; Protein Binding; Protein Structure, Tertiary; Receptors, Laminin - metabolism; single molecule force spectroscopy; specific interactions; Viral Proteins - chemistry; Viral Proteins - metabolism; West Nile virus
• ISSN: 0952-3499; 1099-1352
• DOI: 10.1002/jmr.866

ELISA and Western blot immunochemical data attest an effective and highly specific interaction of the surface glycoprotein E domain II (DII) of the tick born encephalitis and Dengue viruses with the laminin binding protein (LBP). Based on a highly conservative structure of the DII in different flaviviruses we propose a similarly effective interaction between the LBP and the DII of the surface glycoprotein E of the West Nile virus. We report the results of studies of this interaction by immunochemical and single molecule force spectroscopy methods. The specific binding between these species is confirmed by both methods. Copyright © 2007 John Wiley & Sons, Ltd.