title: Proteolysis of bacteriophage phi X174 prohead accessory protein gpB by Escherichia coli OmpT protease is not essential for phage maturation in vivo.
abstract: To examine whether cleavage of the phi X174 prohead accessory protein, gpB, by the OmpT protease is required for phage development in vivo, a phage mutant lacking the OmpT cleavage site and an Escherichia coli C delta ompT strain were constructed. The results of burst size experiments suggest that neither the cleavage site nor the OmpT protein is required for phi X174 development.
authors.affiliation: Department of Biology, University of California, San Diego, California 92093-0322.
authors.forename: M E
authors.initials: ME
authors.lastname: Dalphin
authors.forename: B A
authors.initials: BA
authors.lastname: Fane
authors.forename: M O
authors.initials: MO
authors.lastname: Skidmore
authors.forename: M
authors.initials: M
authors.lastname: Hayashi
mesh_terms: D010584:Bacteriophage phi X 174 / Q000254:growth & development / Q000648:ultrastructure*; D004926:Escherichia coli / Q000201:enzymology; D009024:Morphogenesis; D011499:Protein Processing, Post-Translational; D012697:Serine Endopeptidases / Q000378:metabolism; D014758:Viral Core Proteins / Q000378:metabolism*; D014779:Virus Replication
chemical_list: D014758:Viral Core Proteins; D012697:Serine Endopeptidases; C057840:omptin outer membrane protease