title: Receptor sites for mycoplasmal viruses on Acholeplasma laidlawii.
abstract: All three groups of mycoplasmal viruses tested, MVL1, MVL2, and MVL3, were inactivated by both membranes and lipoglycan from Acholeplasma laidlawii strain JA1. The interaction was specific for components of A. laidlawii since no inactivation occurred with either membrane or lipoglycan from Acholeplasma oculi. Adsorption of virus was proved by the demonstration of radiolabeled virus-lipoglycan or virus-membrane particles that were separable in density gradients from either component alone. Receptors essential for adsorption of MVL2 are part of the oligosaccharide chain of the lipoglycan since deacylation not only did not interfere but actually increased adsorption of virus per unit weight. More complex interactions involving membrane proteins were observed for MVL1 and MVL3.
mesh_terms: D000128:Acholeplasma laidlawii / Q000032:analysis* / Q000378:metabolism; D000327:Adsorption; D001426:Bacterial Proteins / Q000032:analysis; D001435:Bacteriophages / Q000378:metabolism; D001665:Binding Sites / Q000187:drug effects; D002462:Cell Membrane / Q000378:metabolism; D008070:Lipopolysaccharides / Q000378:metabolism; D010447:Peptide Hydrolases / Q000494:pharmacology; D010727:Phosphoric Diester Hydrolases / Q000494:pharmacology; D011991:Receptors, Virus / Q000032:analysis* / Q000378:metabolism; D012997:Solvents / Q000494:pharmacology; D013347:Subcellular Fractions
chemical_list: D001426:Bacterial Proteins; D008070:Lipopolysaccharides; D011991:Receptors, Virus; D012997:Solvents; D010727:Phosphoric Diester Hydrolases; D010447:Peptide Hydrolases