Insights into Lantibiotic Immunity Provided by Bioengineering of LtnI

Draper, Lorraine A.; Deegan, Lucy H.; Hill, Colin; Cotter, Paul D.; Ross, R. Paul

doi:10.1128/aac.00979-12

Cited by 6 publications

(7 citation statements)

References 53 publications

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“…317,462,463 In some cases, a different type of immunity protein cooperates with LanEFG secretion systems such as the NukH protein involved in self-resistance of the nukacin ISK-1 producer. 464−466 …”

Section: Class II Lanthipeptide Biosynthesismentioning

confidence: 99%

“…Many class II lanthipeptide gene clusters also encode LanEFG transporters that were discussed in section 2.7 for class I lanthipeptides, and some encode LanI-like proteins. 317 , 462 , 463 In some cases, a different type of immunity protein cooperates with LanEFG secretion systems such as the NukH protein involved in self-resistance of the nukacin ISK-1 producer. 464 − 466 …”

Section: Class II Lanthipeptide Biosynthesismentioning

confidence: 99%

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Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes

et al. 2017

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Lanthipeptides are ribosomally synthesized and post-translationally modified peptides (RiPPs) that display a wide variety of biological activities, from antimicrobial to antiallodynic. Lanthipeptides that display antimicrobial activity are called lantibiotics. The post-translational modification reactions of lanthipeptides include dehydration of Ser and Thr residues to dehydroalanine and dehydrobutyrine, a transformation that is carried out in three unique ways in different classes of lanthipeptides. In a cyclization process, Cys residues then attack the dehydrated residues to generate the lanthionine and methyllanthionine thioether cross-linked amino acids from which lanthipeptides derive their name. The resulting polycyclic peptides have constrained conformations that confer their biological activities. After installation of the characteristic thioether cross-links, tailoring enzymes introduce additional post-translational modifications that are unique to each lanthipeptide and that fine-tune their activities and/or stability. This review focuses on studies published over the past decade that have provided much insight into the mechanisms of the enzymes that carry out the post-translational modifications.

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Section: Class II Lanthipeptide Biosynthesismentioning

confidence: 99%

Section: Class II Lanthipeptide Biosynthesismentioning

confidence: 99%

Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes

et al. 2017

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“…TMHMM and SPLIT4.0 are most reliable (40), and although there are slight disparities with respect to which amino acid residues are involved in different domains of the protein, both agreed that TrnI possesses two transmembrane regions. Similar TMDs have also been found within the small immunity proteins of lacticin 3147, as well as the sactibiotic propionicin F, while PepI, the immunity protein associated with Pep5, also contains a membrane-associated hydrophobic stretch (41)(42)(43)(44). Such a small immunity protein, most likely associated with the cell membrane because of the presence of the putative TMD sequences, may sequester the thuricin CD peptides or somehow block the insertion of the peptides into the membrane.…”

Section: Discussionmentioning

confidence: 74%

Heterologous Expression of Thuricin CD Immunity Genes in Listeria monocytogenes

Mathur

O’Connor

Cotter

et al. 2014

Antimicrob Agents Chemother

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cBacteriocins are ribosomally synthesized peptides that can have a narrow or broad spectrum of antimicrobial activity. Bacteriocin producers typically possess dedicated immunity systems that often consist of an ATP-binding cassette (ABC) transporter system and/or a dedicated immunity protein. Here we investigated the genes responsible for immunity to thuricin CD, a narrowspectrum two-peptide sactibiotic produced by Bacillus thuringiensis DPC6431. Heterologous expression of putative thuricin CD immunity determinants allowed us to identify and investigate the relative importance of the individual genes and gene products that contribute to thuricin CD immunity. We established that TrnF and TrnG are the individual components of an ABC transporter system that provides immunity to thuricin CD. We also identified a hitherto overlooked open reading frame located upstream of trnF predicted to encode a 79-amino-acid transmembrane protein. We designated this newly discovered gene trnI and established that TrnI alone can provide protection against thuricin CD.

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“…9). LanFE(G) can independently provide lantibiotic immunity, such as LctFEG for lacticin 481 immunity (31), or work synergistically with a membrane-associated protein, such as NisI (32), or a transmembrane protein, such as NukH (9, 10) and LtnI (33). Lantibiotic immunity that is solely provided by transmembrane proteins is very rare.…”

Section: Discussionmentioning

confidence: 99%

ApnI, a Transmembrane Protein Responsible for Subtilomycin Immunity, Unveils a Novel Model for Lantibiotic Immunity

Deng

Zhu

et al. 2014

Appl Environ Microbiol

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Subtilomycin was detected from the plant endophytic strain Bacillus subtilis BSn5 and was first reported from B. subtilis strain MMA7. In this study, a gene cluster that has been proposed to be related to subtilomycin biosynthesis was isolated from the BSn5 genome and was experimentally validated by gene inactivation and heterologous expression. Comparison of the subtilomycin gene cluster with other verified related lantibiotic gene clusters revealed a particular organization of the genes apnI and apnT downstream of apnAPBC, which may be involved in subtilomycin immunity. Through analysis of expression of the apnI and/or apnT genes in the subtilomycin-sensitive strain CU1065 and inactivation of apnI and apnT in the producer strain BSn5, we showed that the single gene apnI, encoding a putative transmembrane protein, was responsible for subtilomycin immunity. To our knowledge, evidence for lantibiotic immunity that is solely dependent on a transmembrane protein is quite rare. Further bioinformatic analysis revealed the abundant presence of ApnI-like proteins that may be responsible for lantibiotic immunity in Bacillus and Paenibacillus. We cloned the paeI gene, encoding one such ApnI-like protein, into CU1065 and showed that it confers resistance to paenibacillin. However, no cross-resistance was detected between ApnI and PaeI, even though subtilomycin and paenibacillin share similar structures, suggesting that the protection provided by ApnI/ApnI-like proteins involves a specific-sequence recognition mechanism. Peptide release/binding assays indicated that the recombinant B. subtilis expressing apnI interacted with subtilomycin. Thus, ApnI represents a novel model for lantibiotic immunity that appears to be common.

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Insights into Lantibiotic Immunity Provided by Bioengineering of LtnI

Cited by 6 publications

References 53 publications

Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes

Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes

Heterologous Expression of Thuricin CD Immunity Genes in Listeria monocytogenes

ApnI, a Transmembrane Protein Responsible for Subtilomycin Immunity, Unveils a Novel Model for Lantibiotic Immunity

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