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Related Experiment Videos

An HlyB-type function is required for expression of the Enterococcus faecalis hemolysin/bacteriocin.

M S Gilmore1, R A Segarra, M C Booth

  • 1Department of Microbiology and Immunology, College of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City 73190.

Infection and Immunity
|December 1, 1990
PubMed
Summary

Researchers sequenced a fragment from Enterococcus faecalis pAD1, identifying CylB, a novel protein similar to E. coli HlyB. This gram-positive bacterium

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Genetics

Background:

  • Enterococcus faecalis pAD1 encodes a hemolysin/bacteriocin.
  • Gram-negative bacteria utilize HlyB-type transport proteins for cytolysin secretion.
  • The presence of similar transport mechanisms in gram-positive bacteria is less understood.

Purpose of the Study:

  • To determine the nucleotide sequence of a key fragment from the E. faecalis pAD1 hemolysin/bacteriocin region.
  • To characterize the protein encoded by this fragment and its functional relationship to known transport proteins.

Main Methods:

  • Nucleotide sequencing of a 3,422-bp restriction fragment from E. faecalis pAD1.
  • In silico analysis to identify open reading frames and infer amino acid sequences.
  • Heterologous expression of the inferred protein (CylB) in E. coli.

Related Experiment Videos

  • Functional complementation assays using insertion mutants.

    • Main Results:

    • A 2,142-bp open reading frame (ORF) was identified, encoding a protein designated CylB.
    • CylB shares significant sequence similarity with HlyB from the E. coli alpha-hemolysin operon.
    • CylB was expressed in E. coli and could complement a mutation in the E. faecalis hemolysin/bacteriocin operon, but not in E. coli hlyB.

    Conclusions:

    • CylB represents the first identified HlyB-type transport protein encoded within a cytolysin determinant from a gram-positive bacterium.
    • While functionally similar to HlyB, CylB exhibits distinct specificity, highlighting evolutionary divergence in transport systems.
    • This finding expands the known distribution of HlyB-type transport functions across bacterial phyla.