Antigenic properties of bacteriophage phi 29 structural proteins.
Serological methods and electron microscopy were used to study the structural proteins of the small Bacillus subtilis bacteriophage phi29. This virus has a large number of fibers attached at both ends of its prolate head. A complex neck assembly is comprised of 12 symmetrically arranged appendages as the outer component. Head fibers, neck appendages, and the head surface bind anti-phi29 antibodies. Immune sera absorbed with defective lysates of suppressor-sensitive (sus) mutants have been used to determine the genetic control of neck appendages production. Studies on the serum-blocking power of lysates defective in different tail components showed that appendages contain the main serum-blocking protein. This finding suggests an essential role of the neck appendages in phage adsorption or DNA injection.
D000327:Adsorption; D000818:Animals; D000936:Antigen-Antibody Complex; D000956:Antigens, Viral / Q000032:analysis; D001412:Bacillus subtilis; D001435:Bacteriophages / Q000254:growth & development / Q000276:immunology*; D001666:Binding Sites, Antibody; D002499:Centrifugation, Density Gradient; D005796:Genes; D007106:Immune Sera; D008242:Lysogeny; D008854:Microscopy, Electron; D009154:Mutation; D011817:Rabbits / Q000276:immunology; D014764:Viral Proteins
D000936:Antigen-Antibody Complex; D000956:Antigens, Viral; D007106:Immune Sera; D014764:Viral Proteins