Literature DB >> 18752624

The amino acid sequences and activities of synergistic hemolysins from Staphylococcus cohnii.

Pawel Mak1, Agnieszka Maszewska, Malgorzata Rozalska.   

Abstract

Staphylococcus cohnii ssp. cohnii and S. cohnii ssp. urealyticus are a coagulase-negative staphylococci considered for a long time as unable to cause infections. This situation changed recently and pathogenic strains of these bacteria were isolated from hospital environments, patients and medical staff. Most of the isolated strains were resistant to many antibiotics. The present work describes isolation and characterization of several synergistic peptide hemolysins produced by these bacteria and acting as virulence factors responsible for hemolytic and cytotoxic activities. Amino acid sequences of respective hemolysins from S. cohnii ssp. cohnii (named as H1C, H2C and H3C) and S. cohnii ssp. urealyticus (H1U, H2U and H3U) were identical. Peptides H1 and H3 possessed significant amino acid homology to three synergistic hemolysins secreted by Staphylococcus lugdunensis and to putative antibacterial peptide produced by Staphylococcus saprophyticus ssp. saprophyticus. On the other hand, hemolysin H2 had a unique sequence. All isolated peptides lysed red cells from different mammalian species and exerted a cytotoxic effect on human fibroblasts.

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Year:  2008        PMID: 18752624     DOI: 10.1111/j.1574-6968.2008.01321.x

Source DB:  PubMed          Journal:  FEMS Microbiol Lett        ISSN: 0378-1097            Impact factor:   2.742


  1 in total

1.  Isolation, biochemical characterization, and cloning of a bacteriocin from the poultry-associated Staphylococcus aureus strain CH-91.

Authors:  Benedykt Wladyka; Katarzyna Wielebska; Marcin Wloka; Oliwia Bochenska; Grzegorz Dubin; Adam Dubin; Pawel Mak
Journal:  Appl Microbiol Biotechnol       Date:  2012-11-30       Impact factor: 4.813

  1 in total

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