Characterization of saturable binding sites for rabies virus.

摘要: A specific, saturable receptor for rabies virus was analyzed on cultured cells of neural or non-neural origin. Viral attachment kinetics were enhanced by DEAE-dextran, an effect which in turn the apparent infectivity inoculum. Under optimized conditions, metabolically labeled ERA strain obeyed laws mass action, whereby amount bound to varied proportionally with concentration virus. Attachment sensitive changes temperature and pH, did not require divalent cations such as Mg2+ Ca2+, occurred despite prior treatment proteolytic sialic acid-specific enzymes. Saturation cell surface could be accomplished 3 X 10(3) 15 attached virions per cell. Competition nonpathogenic variant virus, RV194 -2, vesicular stomatitis Reovirus type 3, another neurotropic failed inhibit binding, West Nile only slightly inhibited suggesting independent cellular receptors recognized these viruses. Isolated glycoprotein compete equivalent manner. However, solubilization BHK-21 octylglucoside yielded a chloroform-methanol-soluble extract blocked attachment. The binding inhibition activity this resistant proteases but destroyed phospholipases neuraminidase, phospholipid glycolipid component at site. These data provide evidence rhabdovirus-common mechanism culture.