Polypeptides and immunoreactivity of empty adenovirus type 1 particles.
Two distinct CsCl-stable empty particle populations were characterized in human adenovirus type 1 infected cells. Different sensitivity to proteases and polypeptide composition indicate that empty capsids A and B are degradation products of two different assembly intermediates. Both empty particle populations react with antihexon antibodies similarly to complete virions. Thus the arrangement of exposed type-specific epitopes is suggested to be unchanged during virus assembly. Experimental evidence is presented that both antifibre and antihexon antibodies trigger structural changes of complete virions, which are initiating the specific loss of core protein V from antibody-aggregated virions.
D000260:Adenoviruses, Human / Q000032:analysis* / Q000276:immunology; D000914:Antibodies, Viral / Q000276:immunology; D002213:Capsid / Q000276:immunology / Q000302:isolation & purification*; D002499:Centrifugation, Density Gradient; D002586:Cesium; D002712:Chlorides; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D010455:Peptides; D012967:Sodium Dodecyl Sulfate; D014771:Virion / Q000276:immunology / Q000302:isolation & purification*
D000914:Antibodies, Viral; D002712:Chlorides; D010455:Peptides; D002586:Cesium; D012967:Sodium Dodecyl Sulfate; C028019:cesium chloride