Proteolysis of bacteriophage phi X174 prohead accessory protein gpB by Escherichia coli OmpT protease is not essential for phage maturation in vivo.
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.
Dalphin
M E
ME
Department of Biology, University of California, San Diego, California 92093-0322.
Fane
B A
BA
Skidmore
M O
MO
Hayashi
M
M
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
D014758:Viral Core Proteins; D012697:Serine Endopeptidases; C057840:omptin outer membrane protease