Literature DB >> 26057793

Overexpression, purification, crystallization and preliminary X-ray diffraction of the nisin resistance protein from Streptococcus agalactiae.

Sakshi Khosa1, Astrid Hoeppner2, Diana Kleinschrodt3, Sander H J Smits1.   

Abstract

Nisin is a 34-amino-acid antimicrobial peptide produced by Lactococcus lactis belonging to the class of lantibiotics. Nisin displays a high bactericidal activity against various Gram-positive bacteria, including some human-pathogenic strains. However, there are some nisin-non-producing strains that are naturally resistant owing to the presence of the nsr gene within their genome. The encoded protein, NSR, cleaves off the last six amino acids of nisin, thereby reducing its bactericidal efficacy. An expression and purification protocol has been established for the NSR protein from Streptococcus agalactiae COH1. The protein was successfully crystallized using the vapour-diffusion method in hanging and sitting drops, resulting in crystals that diffracted X-rays to 2.8 and 2.2 Å, respectively.

Entities:  

Keywords:  Lactococcus lactis; immunity; lantibiotic; lipoprotein; nisin; resistance

Mesh:

Substances:

Year:  2015        PMID: 26057793      PMCID: PMC4461328          DOI: 10.1107/S2053230X15006226

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


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  2 in total

1.  Structural basis of lantibiotic recognition by the nisin resistance protein from Streptococcus agalactiae.

Authors:  Sakshi Khosa; Benedikt Frieg; Daniel Mulnaes; Diana Kleinschrodt; Astrid Hoeppner; Holger Gohlke; Sander H J Smits
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Review 2.  Resistance Mechanisms to Antimicrobial Peptides in Gram-Positive Bacteria.

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Journal:  Front Microbiol       Date:  2020-10-21       Impact factor: 5.640

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