Affiliation:
1. Department of Microbiology, Stellenbosch University, Stellenbosch, South Africa
Abstract
ABSTRACT
Enterococcus faecium
T8, isolated from vaginal secretions of children with human immunodeficiency virus, produces a class IIa
sec
-dependent bacteriocin that is structurally different from three other class IIa
sec
-dependent bacteriocins, i.e., enterocin P and an enterocin P-like bacteriocin, produced by
Enterococcus faecium
, and bacteriocin 31, produced by
Enterococcus faecalis
, and from a class III bacteriocin produced by
E. faecalis
. The genes encoding the bacteriocin, immunity protein, mobilization protein, and relaxase nuclease are located on a 7-kb plasmid. Bacteriocin T8 has a molecular mass of 5.1 kDa based on its DNA sequence, similar to the 5.0 kDa recorded for bacteriocin 31 but larger than the 4.6 kDa reported for enterocin P. At the amino acid level, bacteriocin T8 is 69% homologous to bacteriocin 31 and 47% homologous to enterocin P. Bacteriocin T8 is active against
E. faecalis
isolated from patients diagnosed with vaginosis, against
Lactobacillus sakei
, and against a
Propionibacterium
sp. The peptide is heat stable (60 min at 100°C) and remains active in phosphate buffer from pH 4.0 to 10.0. The mode of activity is bactericidal, as determined with
E. faecalis
.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
51 articles.
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