Previous Article | Next Article ![]()
Antimicrobial Agents and Chemotherapy, May 2009, p. 1964-1973, Vol. 53, No. 5
0066-4804/09/$08.00+0 doi:10.1128/AAC.01382-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Jiale Liu,1
Xiuzhu Chen,1 and
Liandong Huan1*
State Key Laboratory of Microbial Resources, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China,1 Graduate University, Chinese Academy of Sciences, Beijing 100039, China2
Received 15 October 2008/ Returned for modification 8 January 2009/ Accepted 27 February 2009
Nisin is a 34-residue antibacterial peptide produced by Lactococcus lactis that is active against a wide range of gram-positive bacteria. In non-nisin-producing L. lactis, nisin resistance could be conferred by a specific nisin resistance gene (nsr), which encodes a 35-kDa nisin resistance protein (NSR). However, the mechanism underlying NSR-mediated nisin resistance is poorly understood. Here we demonstrated that the protein without the predicted N-terminal signal peptide sequence, i.e., NSRSD, could proteolytically inactivate nisin in vitro by removing six amino acids from the carboxyl "tail" of nisin. The truncated nisin (nisin1-28) displayed a markedly reduced affinity for the cell membrane and showed significantly diminished pore-forming potency in the membrane. A 100-fold reduction of bactericidal activity was detected for nisin1-28 in comparison to that for the intact nisin. In vivo analysis indicated that NSR localized on the cell membrane and endowed host strains with nisin resistance by degrading nisin as NSRSD did in vitro, whereas NSRSD failed to confer resistance upon the host strain. In conclusion, we showed that NSR is a nisin-degrading protease. This NSR-mediated proteolytic cleavage represents a novel mechanism for nisin resistance in non-nisin-producing L. lactis.
Published ahead of print on 9 March 2009.
Present address: Department of Pediatric Dentistry, University of Alabama at Birmingham, Birmingham, AL 35294.
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»