Literature DB >> 23176504

'Bac' to the future: bioengineering lantibiotics for designer purposes.

Evelyn M Molloy1, R Paul Ross, Colin Hill.   

Abstract

Bacteriocins are bacterially produced peptides or proteins that inhibit the growth of other bacterial strains. They can have a broad (effective against multiple genera) or narrow (effective against specific species) spectrum of activity. The diversity of bacteriocins found in Nature, in terms of both spectrum of activity and physiochemical properties, offers the possibility of multiple applications in the food and pharmaceutical industries. However, traditional screening strategies may not provide a sufficient range of natural molecules with specifically desired properties. Research suggests that bioengineering of existing inhibitors has the potential to address this issue, extending the application of natural bacteriocins for use in novel settings and against different targets. In the present paper, we discuss the successful implementation of bioengineering strategies to alter and even improve the functional characteristics of a bacteriocin, using the prototypical lantibiotic nisin as an example. Additionally, we describe the recent use of the nisin-modification machinery in vivo to enhance the properties of medically significant peptides.

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Year:  2012        PMID: 23176504     DOI: 10.1042/BST20120193

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  13 in total

1.  Facile Removal of Leader Peptides from Lanthipeptides by Incorporation of a Hydroxy Acid.

Authors:  Noah A Bindman; Silvia C Bobeica; Wenshe R Liu; Wilfred A van der Donk
Journal:  J Am Chem Soc       Date:  2015-06-01       Impact factor: 15.419

Review 2.  Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.

Authors:  Lindsay M Repka; Jonathan R Chekan; Satish K Nair; Wilfred A van der Donk
Journal:  Chem Rev       Date:  2017-01-30       Impact factor: 60.622

Review 3.  Circular bacteriocins: biosynthesis and mode of action.

Authors:  Christina Gabrielsen; Dag A Brede; Ingolf F Nes; Dzung B Diep
Journal:  Appl Environ Microbiol       Date:  2014-08-29       Impact factor: 4.792

4.  In Vitro Biosynthesis and Substrate Tolerance of the Plantazolicin Family of Natural Products.

Authors:  Caitlin D Deane; Brandon J Burkhart; Patricia M Blair; Jonathan I Tietz; Alice Lin; Douglas A Mitchell
Journal:  ACS Chem Biol       Date:  2016-06-16       Impact factor: 5.100

5.  Engineering unnatural variants of plantazolicin through codon reprogramming.

Authors:  Caitlin D Deane; Joel O Melby; Katie J Molohon; Aziz R Susarrey; Douglas A Mitchell
Journal:  ACS Chem Biol       Date:  2013-07-03       Impact factor: 5.100

6.  Purification and Characterization of a Novel Cold Shock Protein-Like Bacteriocin Synthesized by Bacillus thuringiensis.

Authors:  Tianpei Huang; Xiaojuan Zhang; Jieru Pan; Xiaoyu Su; Xin Jin; Xiong Guan
Journal:  Sci Rep       Date:  2016-10-20       Impact factor: 4.379

7.  Saturation mutagenesis of lysine 12 leads to the identification of derivatives of nisin A with enhanced antimicrobial activity.

Authors:  Evelyn M Molloy; Des Field; Paula M O' Connor; Paul D Cotter; Colin Hill; R Paul Ross
Journal:  PLoS One       Date:  2013-03-11       Impact factor: 3.240

8.  Identification of distinct nisin leader peptide regions that determine interactions with the modification enzymes NisB and NisC.

Authors:  Rustem Khusainov; Gert N Moll; Oscar P Kuipers
Journal:  FEBS Open Bio       Date:  2013-05-30       Impact factor: 2.693

9.  Intensive mutagenesis of the nisin hinge leads to the rational design of enhanced derivatives.

Authors:  Brian Healy; Des Field; Paula M O'Connor; Colin Hill; Paul D Cotter; R Paul Ross
Journal:  PLoS One       Date:  2013-11-11       Impact factor: 3.240

10.  Mechanistic studies on the substrate-tolerant lanthipeptide synthetase ProcM.

Authors:  Subha Mukherjee; Wilfred A van der Donk
Journal:  J Am Chem Soc       Date:  2014-07-08       Impact factor: 15.419

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