structure of Subtilosin A
Microcins are very small bacteriocins, composed of a relatively few peptides. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of E. coli. Subtilosin A is another bacteriocin from Bacillus subtilis. The peptide has a cyclized backbone and forms three cross-links between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22,Thr28 and Phe31.
It is found that these bacteriocins target and eliminate iron-starved pathogens, which is found specifically in an inflamed gut where the E. Coli strain prefer to thrive. Specifically, the protein targets the pathogens are producing iron-scavenging protein in response to a low iron environment. Researchers found. E. coli Nissle’s microcins killed diarrhea-inducing bacteria called Salmonella Enterica in the guts of infected mice. Microcins also helped Nissle outcompete a different, more virulent of E. coli found in the infected mice's guts.
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- Tine Hesman Saey, [https://www.sciencenews.org/article/tiny-toxic-proteins-help-gut-bacteria-defeat-rivals?mode=topic&context=87 "Tiny toxic proteins help gut bacteria defeat rivals "], Science News Magazine Vol. 190, No. 12, December 10, 2016, p. 5
- Hammami R, Zouhir A, Ben Hamida J, Fliss I (2007). "BACTIBASE: a new web-accessible database for bacteriocin characterization". BMC Microbiology. 7: 89. doi:10.1186/1471-2180-7-89. PMC . PMID 17941971.
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