Abstract
BackgroundThe recent increase in bacterial resistance to antibiotics has promoted the exploration of novel antibacterial materials. As a result, many researchers are undertaking work to identify new lantibiotics because of their potent antimicrobial activities. The objective of this study was to provide details of a lantibiotic-like gene cluster in Paenibacillus elgii B69 and to produce the antibacterial substances coded by this gene cluster based on culture screening.ResultsAnalysis of the P. elgii B69 genome sequence revealed the presence of a lantibiotic-like gene cluster composed of five open reading frames (elgT1, elgC, elgT2, elgB, and elgA). Screening of culture extracts for active substances possessing the predicted properties of the encoded product led to the isolation of four novel peptides (elgicins AI, AII, B, and C) with a broad inhibitory spectrum. The molecular weights of these peptides were 4536, 4593, 4706, and 4820 Da, respectively. The N-terminal sequence of elgicin B was Leu-Gly-Asp-Tyr, which corresponded to the partial sequence of the peptide ElgA encoded by elgA. Edman degradation suggested that the product elgicin B is derived from ElgA. By correlating the results of electrospray ionization-mass spectrometry analyses of elgicins AI, AII, and C, these peptides are deduced to have originated from the same precursor, ElgA.ConclusionsA novel lantibiotic-like gene cluster was shown to be present in P. elgii B69. Four new lantibiotics with a broad inhibitory spectrum were isolated, and these appear to be promising antibacterial agents.
Highlights
The recent increase in bacterial resistance to antibiotics has promoted the exploration of novel antibacterial materials
Not all type AI lantibiotic-like gene clusters contain all these genes; for example, in the gene cluster spaBTCAIFGRK [12], which codes for the biosynthesis of subtilin, the function of LanP is replaced by an intrinsic protease of Bacillus subtilis ATCC 6633 [13]
We present the detailed bioinformatic analysis of a novel lantibiotic-like gene cluster in the Paenibacillus elgii B69 genome
Summary
The recent increase in bacterial resistance to antibiotics has promoted the exploration of novel antibacterial materials. Two major types of bacteriocins can be distinguished according to their posttranslational modifications: Class I, the modified bacteriocins or lantibiotics, and Class II, the unmodified bacteriocins. Lantibiotics are a group of small (< 5 kDa) modified bacteriocins characterized by the presence of unusual amino acids such as the thioether-bridge-containing amino acids lanthionine (Lan) and methyllanthionine (MeLan), and several dehydrated amino acids such as a,b-didehydroalanine (Dha) and a,b-didehydrobutyrine (Dhb). The typical gene cluster of type AI lantibiotics, such as nisin and epidermin, includes the structural gene lanA, modification enzyme-encoding genes lanB and lanC, the processing protease-encoding gene lanP, the transporter gene lanT, and the immunity genes lanI and/or lanEFG. Not all type AI lantibiotic-like gene clusters contain all these genes; for example, in the gene cluster spaBTCAIFGRK [12], which codes for the biosynthesis of subtilin, the function of LanP is replaced by an intrinsic protease of Bacillus subtilis ATCC 6633 [13]
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
