title: Amino acids in pneumolysin important for hemolytic activity identified by random mutagenesis.
abstract: The structural gene of pneumolysin was randomly mutagenized. A screen, developed to identify mutants with reduced hemolytic activity, identified substitutions within the cysteine-containing region and also at residues toward the N terminus of the toxin. These are the first reported changes within the N-terminal region of the toxin that affect cytolytic activity.
authors.affiliation: Department of Microbiology, University of Leicester, United Kingdom.
authors.forename: J
authors.initials: J
authors.lastname: Hill
authors.forename: P W
authors.initials: PW
authors.lastname: Andrew
authors.forename: T J
authors.initials: TJ
authors.lastname: Mitchell
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001426:Bacterial Proteins; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D006461:Hemolysis; D066298:In Vitro Techniques; D016296:Mutagenesis; D017354:Point Mutation; D012756:Sheep; D013296:Streptococcus pneumoniae / Q000235:genetics / Q000472:pathogenicity; D013301:Streptolysins / Q000235:genetics* / Q000633:toxicity*; D014774:Virulence / Q000235:genetics
chemical_list: D001426:Bacterial Proteins; D013301:Streptolysins; C032290:plY protein, Streptococcus pneumoniae