Garvicin A, a Novel Class IId Bacteriocin from Lactococcus garvieae That Inhibits Septum Formation in L. garvieae Strains

Maldonado‐Barragán, Antonio; Cárdenas, Nívia; Martínez, Beatriz; Ruiz-Barba, José Luis; Fernández‐Garayzábal, J. F.; Rodríguez, Juan M.; Gibello, Alicia

doi:10.1128/aem.00830-13

Cited by 55 publications

(53 citation statements)

References 63 publications

(68 reference statements)

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“…Garvicin A is a 43-residue class IId bacteriocin produced by L. garvieae 21881 (human clinical isolate) with a mass of 4.7 kDa. It has a narrow antimicrobial spectrum (33). Garvicin KS, the bacteriocin identified in the present study, is different from the aforementioned bacteriocins in composition.…”

Section: Discussioncontrasting

confidence: 65%

Novel Group of Leaderless Multipeptide Bacteriocins from Gram-Positive Bacteria

Ovchinnikov

Chi

Mehmeti

et al. 2016

Appl Environ Microbiol

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From raw milk we found 10 Lactococcus garvieae isolates that produce a new broad-spectrum bacteriocin. Though the isolates were obtained from different farms, they turned out to possess identical inhibitory spectra, fermentation profiles of sugars, and repetitive sequence-based PCR (rep-PCR) DNA patterns, indicating that they produce the same bacteriocin. One of the isolates (L. garvieae KS1546) was chosen for further assessment. Purification and peptide sequencing combined with genome sequencing revealed that the antimicrobial activity was due to a bacteriocin unit composed of three similar peptides of 32 to 34 amino acids. The three peptides are produced without leader sequences, and their genes are located next to each other in an operon-like structure, adjacent to the genes normally involved in bacteriocin transport (ABC transporter) and self-immunity. The bacteriocin, termed garvicin KS (GarKS), showed sequence homology to four multipeptide bacteriocins in databases: the known staphylococcal aureocin A70, consisting of four peptides, and three unannotated putative multipeptide bacteriocins produced by Bacillus cereus. All these multipeptide bacteriocin loci show conserved genetic organization, including being located adjacent to conserved genetic determinants (Cro/cI and integrase) which are normally associated with mobile genetic elements or genome rearrangements. The antimicrobial activity of all multipeptide bacteriocins was confirmed with synthetic peptides, and all were shown to have broad antimicrobial spectra, with GarKS being the most active of them. The inhibitory spectrum of GarKS includes important pathogens belonging to the genera Staphylococcus, Bacillus, Listeria, and Enterococcus. IMPORTANCEBacterial resistance to antibiotics is a very serious global problem. There are no new antibiotics with novel antimicrobial mechanisms in clinical trials. Bacteriocins use antimicrobial mechanisms different from those of antibiotics and can kill antibioticresistant bacteria, but the number of bacteriocins with very broad antimicrobial spectra is very small. In this study, we have found and purified a novel three-peptide bacteriocin, garvicin KS. By homology search, we were able to find one known and three novel sequence-related bacteriocins consisting of 3 or 4 peptides. None of the peptides has modified amino acids in its sequence. Thus, the activity of all bacteriocins was confirmed with chemically synthesized peptides. All of them, especially garvicin KS, have very broad antibacterial spectra, thus representing a great potential in antimicrobial applications in the food industry and medicine.

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Section: Discussioncontrasting

confidence: 65%

Novel Group of Leaderless Multipeptide Bacteriocins from Gram-Positive Bacteria

Ovchinnikov

Chi

Mehmeti

et al. 2016

Appl Environ Microbiol

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“…Addition of antibiotics during cytokinesis results in the development of a bulge and inhibition of the cell cycle[3]. Two bacteriocins, garvicin A and lactococcin 972, have thus far been shown to have this mechanism of action[79,80]. Garvicin A is specifically active against other Lactococcus garvieae strains, whilst lactococcin 972 inhibits only closely related Lactococcus spp.…”

mentioning

confidence: 98%

Bacteriocins and their position in the next wave of conventional antibiotics

Cavera

Arthur

Kashtanov

et al. 2015

International Journal of Antimicrobial Agents

159

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“…Three clusters contained β‐hairpins and were combined and joined with a single modeled β‐hairpin structure (Odorranain M1, AP01300) 72 left unassigned by the original clustering. One experimental structure (Mytilin B, PDB code 2EEM) from this group was reassigned to a group of two combined clusters containing αββ folds joined by two modeled structures left unassigned, one αββ (Garvicin A, AP02402) the other βαβ (Rattusin, AP02178) . Four helix hairpins that were left unassigned, namely experimental structures of Sublancin 168 (PDB code 2MIJ), Thurincin H (2LBZ), Thuricin CD (2L9X), and EcAMP1 (2L2R), were joined with two clusters containing a continuum of v‐shaped, helix‐kink‐helix and helix hairpin structures.…”

Section: Resultsmentioning

confidence: 99%

Large scale ab initio modeling of structurally uncharacterized antimicrobial peptides reveals known and novel folds

et al. 2018

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Antimicrobial resistance within a wide range of infectious agents is a severe and growing public health threat. Antimicrobial peptides (AMPs) are among the leading alternatives to current antibiotics, exhibiting broad spectrum activity. Their activity is determined by numerous properties such as cationic charge, amphipathicity, size, and amino acid composition. Currently, only around 10% of known AMP sequences have experimentally solved structures. To improve our understanding of the AMP structural universe we have carried out large scale ab initio 3D modeling of structurally uncharacterized AMPs that revealed similarities between predicted folds of the modeled sequences and structures of characterized AMPs. Two of the peptides whose models matched known folds are Lebocin Peptide 1A (LP1A) and Odorranain M, predicted to form β-hairpins but, interestingly, to lack the intramolecular disulfide bonds, cation-π or aromatic interactions that generally stabilize such AMP structures. Other examples include Ponericin Q42, Latarcin 4a, Kassinatuerin 1, Ceratotoxin D, and CPF-B1 peptide, which have α-helical folds, as well as mixed αβ folds of human Histatin 2 peptide and Garvicin A which are, to the best of our knowledge, the first linear αββ fold AMPs lacking intramolecular disulfide bonds. In addition to fold matches to experimentally derived structures, unique folds were also obtained, namely for Microcin M and Ipomicin. These results help in understanding the range of protein scaffolds that naturally bear antimicrobial activity and may facilitate protein design efforts towards better AMPs.

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Garvicin A, a Novel Class IId Bacteriocin from Lactococcus garvieae That Inhibits Septum Formation in L. garvieae Strains

Cited by 55 publications

References 63 publications

Novel Group of Leaderless Multipeptide Bacteriocins from Gram-Positive Bacteria

Novel Group of Leaderless Multipeptide Bacteriocins from Gram-Positive Bacteria

Bacteriocins and their position in the next wave of conventional antibiotics

Large scale ab initio modeling of structurally uncharacterized antimicrobial peptides reveals known and novel folds

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