Demonstration of low molecular weight polypeptides associated with small, round-structured viruses by western immunoblot analysis.
Small, round-structured viruses (SRSV) were detected in 14 of 300 fecal specimens obtained from patients with acute gastroenteritis by electron microscopy. These SRSV strains were morphologically indistinguishable from one another. While 11 of these strains had a single usual major structural protein with molecular weight of 63,000 (63K) daltons (p63), interestingly, three strains possessed a single major structural protein with molecular weight of 33K daltons (p33). Treatments of p63-SRSV with proteolytic enzymes or denaturating reagents did not affect the molecular weight of p63, and the p33 was not detectable by Western immunoblot in the ultracentrifugal supernatant of the p63-SRSV suspension. These results suggest that the p33 is neither a definitive subunit of p63 nor disintegrated component derived from the p63-SRSV but a novel polypeptide of SRSV. Immune electron microscopy and Western immunoblot analyses indicated that p63- and p33-SRSVs may share an antigenic determinant(s).
D000208:Acute Disease; D015153:Blotting, Western; D003429:Cross Reactions; D000939:Epitopes / Q000276:immunology; D005243:Feces / Q000382:microbiology; D005759:Gastroenteritis / Q000382:microbiology; D006801:Humans; D008970:Molecular Weight; D009663:Norwalk virus / Q000737:chemistry* / Q000302:isolation & purification / Q000648:ultrastructure; D010455:Peptides / Q000737:chemistry; D015678:Viral Structural Proteins / Q000032:analysis* / Q000737:chemistry / Q000276:immunology; D014777:Virus Diseases / Q000382:microbiology
D000939:Epitopes; D010455:Peptides; D015678:Viral Structural Proteins