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  • Lactobacillus proteins are associated with the bactericidal activity against E. coli of female genital tract secretions.

Lactobacillus proteins are associated with the bactericidal activity against E. coli of female genital tract secretions.

PloS one (2012-11-28)
Sabah Kalyoussef, Edward Nieves, Ellen Dinerman, Colleen Carpenter, Viswanathan Shankar, Jamie Oh, Berta Burd, Ruth H Angeletti, Karen W Buckheit, David N Fredricks, Rebecca P Madan, Marla J Keller, Betsy C Herold
ABSTRACT

Female genital tract secretions are bactericidal for Escherichia (E.) coli ex vivo. However, the intersubject variability and molecules that contribute to this activity have not been defined. The bactericidal activity and concentration of immune mediators in cervicovaginal lavage (CVL) collected from 99 healthy women were determined. CVL reduced the number of E. coli colonies by 68% [-26, 100] (median [range]). CVL were active against laboratory and clinical isolates of E. coli, but were inactive against Lactobacillus species. Bactericidal activity correlated with the concentration of protein recovered (p<0.001), but not with cytokines, chemokines or antimicrobial peptides. Four CVL with>90% inhibitory activity (active) and two with<30% activity were subjected to MS/MS proteomic analysis. 215 proteins were identified and six were found exclusively in active samples. Four of these corresponded to Lactobacillus crispatus or jensenii proteins. Moreover, culture supernatants from Lactobacillus jensenii were bactericidal for E. coli. Both host and commensal microbiota proteins contribute to mucosal defense. Identification of these proteins will facilitate the development of strategies to maintain a healthy vaginal microbiome and prevent colonization with pathogenic bacteria such as E. coli that increase the risk for urinary tract infections, preterm labor and perinatal infection.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Proteinase K from Tritirachium album, buffered aqueous glycerol solution, for molecular biology, ≥800 units/mL
Sigma-Aldrich
Proteinase K from Tritirachium album, lyophilized powder, BioUltra, ≥30 units/mg protein, for molecular biology
Sigma-Aldrich
Proteinase K from Tritirachium album, lyophilized powder, ≥30 units/mg protein
Sigma-Aldrich
Proteinase K from Tritirachium album, ≥3.0 unit/mg solid, lyophilized powder
Sigma-Aldrich
Proteinase K from Tritirachium album, ≥500 units/mL, buffered aqueous glycerol solution