Two-peptide bacteriocins

Precursor protein that produces the cyclic trypsin inhibitor SFTI-1 Two-peptide bacteriocin plantaracin EF Lei4P... 

Class II bacteriocins can be further divided into four groups based on structural features pediocin-like bacteriocins, two-peptide bacteriocins, cyclic bacteriocins and linear non-pediocin-like one-peptide bacteriocins. NMR has been used to characterise examples from each of these subgroups. 

Pediocin ST18 have been partially purified by ammonium sulphate precipitation, followed by separation in a Sep-Pack C18 column and reverse-phase HPLC on a C18 Nucleosil column, and yielded in two active antimicrobial peptides, which suggests that pediocin ST18 may be a two-peptide bacteriocin. The peptide had bacteriostatic... 

Petersen, F.C., Fimland, G., and Scheie, A.A. (2006). Purification and functional studies of a potent modified quorum-sensing peptide and a two-peptide bacteriocin in Streptococcus mutans. Mol Microbiol 61, 1322-1334. 

Peptide bacteriocins produced by lactic acid bacteria are categorized into two different classes according to their biochemical and genetic properties (Drider et al. 2006 Nes et al. 2007). Class I peptides are the lantibiotics, which are small, post-translationally modified peptides that contain unusual amino acids such as lanthionine (TC 1.C.20). Class II includes unmodified bacteriocins that are subdivided into three subclasses, namely, class Ha (pediocin-like bacteriocins), class Ilb (two-peptide bacteriocins), and He (other (i.e., non-pediocin-like), one-peptide bacteriocins). 

Stephens, S.K., Horiano, B., Cathcart, D.P, et al. (1998) Molecular analysis of the locus responsible for production of plantaricin S, a two-peptide bacteriocin produced by Lactobacillusplantarum LPCOIO. Appl Environ Microbiol 64, 1871-1877. 

From the ileal-caecal region of the human GI tract, a probiotic Lact. salivarius subsp. salivarius was isolated and found to produce the two-peptide bacteriocin ABP-118, which is discussed at the... 

Kjos, M., Oppegard, C., Diep, D.B., et al. (2014). Sensitivity to the two-peptide bacteriocin lactococcin G is dependent on UppP, an enzyme involved in cell-wall synthesis. Mol Microbiol 92, 1177-1187. 

Liu, X., Vederas, J.C., Whittal, R.M., et al. (2011). Identification of an N-terminal formylated, two-peptide bacteriocin from Enterococcus faecalis 710C. JAgric Food Chem 59, 5602-5608. 

Ringitore, E.V., Hebert, E.M., Nader-Macias, M.E., and Sesma, F. (2009). Characterization of sahvaridn CRL 1328, a two-peptide bacteriocin produced by Lactobacillus salivarius CRL 1328 isolated from the human vagina. Res Microbiol 160, 401-408. 

Rogne, R, Haugen, C., Eimland, G., et al. (2009). Three-dimensional structure of the two-peptide bacteriocin planta-ridn JK. Peptides 30, 1613—1621. 

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