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 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.
State Research Center of Virology and Biotechnology , Koltsovo, Novosibirsk Region 630559, Russia.
Maria V
MV
Bogachek
Elena V
EV
Protopopova
Valery B
VB
Loktev
Boris N
BN
Zaitsev
Mélanie
M
Favre
Sergey K
SK
Sekatskii
Giovanni
G
Dietler
D000911:Antibodies, Monoclonal; D001696:Biomechanical Phenomena; D015153:Blotting, Western; D006023:Glycoproteins / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D007124:Immunoenzyme Techniques; D007150:Immunohistochemistry; D018625:Microscopy, Atomic Force; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D017474:Receptors, Laminin / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry* / Q000378:metabolism*; D014902:West Nile virus
D000911:Antibodies, Monoclonal; D006023:Glycoproteins; D010455:Peptides; D017474:Receptors, Laminin; D014764:Viral Proteins