1.C.30 The Plantaricin JK (Plantaricin JK) Family

Many organisms synthesize proteins (or peptides) which are degraded to relatively small hydrophobic or amphipathic, bioactive peptides. These peptides exhibit antibiotic, fungicidal, virucidal, hemolytic and/or tumoricidal activities by interacting with membranes and forming transmembrane channels that allow the free flow of electrolytes, metabolites and water across the phospholipid bilayers. Most of these peptides appear to function in biological warfare. There are many designations given to these bioactive peptides. They include the magainins, cecropins, melittins, defensins, bacteriocidins, etc. The proteins in each family within this functional superfamily are homologous, but they exhibit little or no significant sequence similarity with members of the other families. Thus, each family may have evolved independently. However, certain common structural features observed between members of distinct families suggest that at least some of these families share a common ancestry.

The generalized transport reaction catalyzed by channel-forming amphipathic peptides is:

small solutes, electrolytes and water (in) small solutes, electrolytes and water (out).

Bacteriocins are bacterially produced peptide antibiotics with the ability to kill a limited range of bacteria, usually but not always those that are closely related to the producer bacterium. Many of them exhibit structural features typical of members of the eukaryotic channel-forming amphipathic peptides. That is, they are usually synthesized as small precursor proteins or peptides which are processed with proteolytic elimination of their N-terminal leader sequences, and the resultant mature peptides form one, two or more putative amphipathic transmembrane α-helical spanners (TMSs). For those with two TMSs, a characteristic hinge region that separates the two putative transmembrane segments is usually observed. A similar structural arrangement occurs in the two-TMS Cecropin A proteins (TC #1.C.17).

Many bacteriocins are encoded in operons that also encode an immunity protein and an ABC transport system (TC #3.A.1) with a protease domain at the N-terminus. The ABC systems export the bacteriocins while the protease domains cleave the N-terminal leader sequence. A few bacteriocins are exported by the type II general secretory pathway rather than by ABC-type export systems. In some cases, expression of the bacteriocin-encoding operon is induced by a bacteriocin-like peptide which acts in conjunction with a two component sensor kinase-response regulator to effect induction.

IIb, Poration complexes requiring two peptides for activity.

Many bacteriocins have been identified in addition to those tabulated in the TC system, but those listed are among the best characterized, with respect to evidence for channel formation in target bacterial membranes. Class III and IV bacteriocins (Klaenhammer, 1993) are large heat-labile proteins that function by mechanisms unrelated to those of the bacteriocins listed here.



This family belongs to the Bacterial Bacteriocin (BB) Superfamily.

 

References:

Ahn S.J., R.A. Burne. (2006). The atlA operon of Streptococcus mutans: role in autolysin maturation and cell surface biogenesis. J. Bacteriol. 188: 6877-6888.

Allison, G.E., C. Fremaux and T.R. Klaenhammer (1994). Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J. Bacteriol. 176: 2235-2241.

Bengtsson, T., B. Zhang, R. Selegård, E. Wiman, D. Aili, and H. Khalaf. (2017). Dual action of bacteriocin PLNC8 αβ through inhibition of Porphyromonas gingivalis infection and promotion of cell proliferation. Pathog Dis 75:.

Diep, D.B., L.S. Håvarstein and I.F. Nes (1995). A bacteriocin-like peptide induces bacteriocin synthesis in Lactobacillus plantarum C11. Mol. Microbiol. 18: 631-639.

Klaenhammer, T.R. (1993). Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol. Rev. 12: 39-85.

Moll, G.N., E. van den Akker, H.H. Hauge, J. Nissen-Meyer, I.F. Nes, W.N. Konings and A.J.M. Driessen (1999). Complementary and overlapping selectivity of the two-peptide bacteriocins plantaricin EF and JK. J. Bacteriol. 181: 4848-4852.

Moll, G.N., W.N. Konings and A.J.M. Driessen (1999). Bacteriocins: mechanism of membrane insertion and pore formation. Antonie van Leeuwenhoek 76: 185-198.

Nes, I.F., D.B. Diep, L.S. Håvarstein, M.B. Brurberg, V. Eijsink and H. Holo (1996). Biosynthesis of bacteriocins in lactic acid bacteria. Antonie van Leeuwenhoek 70: 113-128.

Oppegård, C., P. Rogne, L. Emanuelsen, P.E. Kristiansen, G. Fimland, and J. Nissen-Meyer. (2007). The two-peptide class II bacteriocins: structure, production, and mode of action. J. Mol. Microbiol. Biotechnol. 13: 210-219.

Sahl, H.-G. and G. Bierbaum (1998). Lantibiotics: biosynthesis and biological activities of uniquely modified peptides from Gram-positive bacteria. Annu. Rev. Microbiol. 52: 41-79.

Sharma, A. and S. Srivastava. (2014). Anti-Candida activity of two-peptide bacteriocins, plantaricins (Pln E/F and J/K) and their mode of action. Fungal Biol 118: 264-275.

Venema, K., G. Venema and J. Kok (1995). Lactococcal bacteriocins: mode of action and immunity. Trends Microbiol. 3: 299-304.

Examples:

TC#NameOrganismal TypeExample
1.C.30.1.1

Anion-selective class IIb two peptide bacteriocin, plantaricin J, K (Oppegard et al., 2007).  Causes loss of the pmf, K+ loss and initiation of apoptosis in Candida (Sharma and Srivastava 2014).

Gram-positive bacteria

PlnJ, K of Lactobacillus plantarum

 
1.C.30.1.2Plantaricins Sb, Sa precursors Gram-positive bacteria Plantaricin Sb, Sa of Lactobacillus plantarum
 
1.C.30.1.3Thermophilin 1, 2, precursors ThmA, B (may participate in autolysin maturation and cell surface biogenesis (Ahn and Burne, 2006)).Gram-positive bacteria ThmA, B of Streptococcus thermophilus
 
1.C.30.1.4

Uncharacterized plantaricin of 60 aas and 1 TMS

UP of Leuconostoc citreum

 
1.C.30.1.5

Uncharacterized bacteriocin

Bacteriocin of Streptococcus suis R61

 
1.C.30.1.6

Two component bacteriocin, plantaricin NC8, PLNC8 αβ.  The precursor of alpha is 47 aas and the last 29 aas comprise the active pore-forming bacteriocin subunit (0 TMSs); the precursor of beta is 55 aas and the last 34 aas comprise the active pore-forming bacteriocin subunit (1 TMS).  It exerts dual action  through inhibition of Porphyromonas gingivalis infection and promotion of cell proliferation (Bengtsson et al. 2017).

 

PLNC8 of Lactobacillus plantarum