Adsorption of bacteriophage phi 29 to Bacillus subtilis through the neck appendages of the viral particle.
Phage phi 29 particles produced under restrictive conditions by mutants in gene 12 have normal amounts of all of the structural proteins except the appendage protein, p12*, which is missing. These particles are not infective and do not adsorb to Bacillus subtilis cells. By in vitro complementation of 12- particles with extracts containing protein p12* or with purified protein p12*, the defective particles could bind the appendage protein and become infective and able to adsorb to bacteria. Therefore, the neck appendages of phage phi 29, formed by protein p12*, are involved in the interaction of the phage with the cell wall receptors. Protein p12*, purified in its native state, competed with wild-type phage for adsorption to bacteria. Also, protein p12* could displace adsorbed phage from bacteria. Since the displaced phage was infective, protein p12* does not seem to be modified after phage adsorption.
D000327:Adsorption; D001435:Bacteriophages / Q000378:metabolism* / Q000648:ultrastructure; D001667:Binding, Competitive; D011991:Receptors, Virus / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D011991:Receptors, Virus; D014764:Viral Proteins