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Mol Gen Mikrobiol Virusol ; (4): 36-9, 2003.
Article in Russian | MEDLINE | ID: mdl-14664162

ABSTRACT

The interaction of the VEE virus virions with human LBP was investigated. The affinely purified 43 kDa recombinant LBP (rLBP) of man was found to interact effectively with the VEE virus virions purified in immune enzyme assay. The affinity constant of 43 kDa rLBP with virions was equal to 4.3-4.8 x 10(7) M-1. The rabbit antiviral polyclonal antibodies blocked the interaction of rLBP with the VEE virus virions. According to Western blot, rLBP is capable of interacting with the E1 glycoprotein of the VEE virus, which suggests the presence of a specific epitope of binding with LBP in the surface of the E1-E2 heterodimer of the VEE virus. The results confirm that human LBP could be a receptor for the VEE virus.


Subject(s)
Encephalitis Virus, Venezuelan Equine/metabolism , Protein Precursors/metabolism , Receptors, Laminin/metabolism , Virion/metabolism , Animals , Blotting, Western , Encephalitis Virus, Venezuelan Equine/immunology , Encephalomyelitis, Venezuelan Equine/virology , Epitopes , Glycoproteins/metabolism , Horse Diseases/virology , Horses , Humans , Protein Precursors/genetics , Rabbits , Receptors, Laminin/genetics , Recombinant Proteins/genetics , Recombinant Proteins/metabolism , Viral Envelope Proteins/metabolism , Virion/immunology
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