Chemotaxis to oligopeptides by Pseudomonas aeruginosa.
A number of peptides were evaluated as chemoattractants for Pseudomonas aeruginosa. Several strains recognized tri-, tetra-, penta-, and hexapeptides in a capillary tube assay. Tripeptides altered at the carboxyl terminus were good attractants, whereas tripeptides altered at the amino terminus did not serve as chemoattractants. Methionine-containing peptides were relatively poor attractants. Arginine-containing peptides gave the best responses. Reduced responses to larger peptides suggest that porin penetration is required. No extracellular peptidase activity was detected. We conclude that oligopeptides are good attractants and that specificity for chemotactic recognition of oligopeptides exists.
Kelly-Wintenberg
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Department of Microbiology, University of Tennessee, Knoxville 37996-0856.
Montie
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D000595:Amino Acid Sequence; D001693:Biological Transport, Active; D002633:Chemotaxis / Q000187:drug effects* / Q000502:physiology; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000493:pharmacokinetics / Q000494:pharmacology*; D011550:Pseudomonas aeruginosa / Q000187:drug effects* / Q000502:physiology*; D013329:Structure-Activity Relationship
D009842:Oligopeptides