STRUCTURE:
Reutericin 6, a bacteriocin produced by Lactobacillus reuteri LA6 that was isolated from the faeces of a human infant at 2 months of age, was purified to homogeneity from broth culture-supernatant by reverse-phase chromatography. Molecular weight (5652) by mass spectrometry and primary structure of reutericin 6 were identical to that of gassericin A produced by Lactobacillus gasseri LA39 which was isolated from the faeces of the same human infant at 4 months old. Reutericin 6 was shown to be a class II and cyclic bacteriocin. PCR amplification on the chromosome DNA of L. reuteri LA6 as a template with the primers based on the DNA sequences cloned (gassericin A and acidocin B from Lactobacillus acidophilus M46) and sequencing revealed that L. reuteri LA6 has the structural gene for gassericin A with no variations among those primers. These results indicate that a bacteriocin of the same structure has been produced by different lactobacilli species isolated from the same infant.
ACTIVITY:
gassericin A inhibited the growth of L. reuteri LA6, but reutericin 6, which has a narrower spectrum than gassericin A, did not inhibit the growth of Lactobacillus gasseri LA39.
Mammalian : 20 hour Yeast : 30 min E. coli : >10 hour
Extinction Coefficient
19490 M-1 cm-1
Absorbance 280nm
219.12
Red solid plot : values according to the hydrophobicity scale of Kyte and Doolittle (reference paper).
Yellow dashed plot : Experimentally determined hydrophobicity scale for proteins at membrane interfaces(reference paper).
Green dotted-dashed plot : prediction of transmembrane helices (reference paper). In this scale (unlike the others), more negative values reflect greater hydrophobicity.
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