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

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 flavi...

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Bibliographic Details
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
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Summary: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.
ISSN:0952-3499
1099-1352
DOI:10.1002/jmr.866