The DOI matches its Crossref record; 208 of the 208 references it cites were found in a registry or an index.
Review: Bacteriocins of Lactic Acid Bacteria
Abstract
During the last few years, a large number of new bacteriocins produced by lactic acid bacteria (LAB) have been identified and characterized. LAB-bacteriocins comprise a heterogeneous group of physicochemically diverse ribosomally-synthesized peptides or proteins showing a narrow or broad antimicrobial activity spectrum against Gram-positive bacteria. Bacteriocins are classified into separate groups such as the lantibiotics (Class I); the small (<10 kDa) heat-stable postranslationally unmodified non-lantibiotics (Class II), further subdivided in the pediocin-like and anti Listeria bacteriocins (subclass IIa), the two-peptide bacteriocins (subclass IIb), and the sec-dependent bacteriocins (subclass IIc); and the large (>30 kDa) heat-labile non-lantibiotics (Class III). Most bacteriocins characterized to date belong to Class II and are synthesized as precursor peptides (preprobacteriocins) containing an N-terminal double-glycine leader peptide, which is cleaved off concomitantly with externalization of biologically active bacteriocins by a dedicated ABC-transporter and its accessory protein. However, the recently identified sec-dependent bacteriocins contain an N-terminal signal peptide that directs bacteriocin secretion through the general secretory pathway (GSP). Most LAB-bacteriocins act on sensitive cells by destabilization and permeabilization of the cytoplasmic membrane through the formation of transitory poration complexes or ionic channels that cause the reduction or dissipation of the proton motive force (PMF). Bacteriocin producing LAB strains protect themselves against the toxicity of their own bacteriocins by the expression of a specific immunity protein which is generally encoded in the bacteriocin operon. Bacteriocin production in LAB is frequently regulated by a three-component signal transduction system consisting of an induction factor (IF), and histidine protein kinase (HPK) and a response regulator (RR). This paper presents an updated review on the general knowledge about physicochemical properties, molecular mode of action, biosynthesis, regulation and genetics of LAB-bacteriocins.
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Cites
ABC Transporters: From Microorganisms to Man
Higgins, C. F. (1992) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.08.110192.000435 · Cited by 3,985
Bacteriocins of gram-positive bacteria
Jack, R. W., Tagg, J. R., & Ray, B. (1995) · Microbiological Reviews · doi:10.1128/mr.59.2.171-200.1995 · Cited by 2,711
Genetics of bacteriocins produced by lactic acid bacteria
Klaenhammer, T. (1993) · FEMS Microbiology Reviews · doi:10.1016/0168-6445(93)90057-g · Cited by 2,029
The complete general secretory pathway in gram-negative bacteria
Pugsley, A. P. (1993) · Microbiological Reviews · doi:10.1128/mmbr.57.1.50-108.1993 · Cited by 1,774
Bacteriocins of lactic acid bacteria
Klaenhammer, T. R. (1988) · Biochimie · doi:10.1016/0300-9084(88)90206-4 · Cited by 1,539
Antibacterial activity of Lactobacillus sake isolated from meat
Schillinger, U., & L�cke, F. K. (1989) · Applied and Environmental Microbiology · doi:10.1128/aem.55.8.1901-1906.1989 · Cited by 1,330
Perlman, D., & Halvorson, H. O. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80341-6 · Cited by 1,131
Lactic acid bacteria of foods and their current taxonomy
Stiles, M. E., & Holzapfel, W. H. (1997) · International Journal of Food Microbiology · doi:10.1016/s0168-1605(96)01233-0 · Cited by 1,106
Applications of the bacteriocin, nisin
Delves-Broughton, J., Blackburn, P., Evans, R. J., & Hugenholtz, J. (1996) · Antonie van Leeuwenhoek · doi:10.1007/bf00399424 · Cited by 972
Kleerebezem, M., Quadri, L. E. N., Kuipers, O. P., & De Vos, W. M. (1997) · Molecular Microbiology · doi:10.1046/j.1365-2958.1997.4251782.x · Cited by 790
Cited by
Bacteriocins from lactic acid bacteria: purification, properties and use as biopreservatives
Parada, J. L., Caron, C. R., Medeiros, A. B. P., & Soccol, C. R. (2007) · Brazilian Archives of Biology and Technology · doi:10.1590/s1516-89132007000300018 · Cited by 357
Antimicrobial potential of bacteriocins: in therapy, agriculture and food preservation
Ahmad, V., Khan, M. S., Jamal, Q. M. S., Alzohairy, M. A., Al Karaawi, M. A., & Siddiqui, M. U. (2017) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2016.08.016 · Cited by 293
Use of nisin and other bacteriocins for preservation of dairy products
Sobrino-López, A., & Martín-Belloso, O. (2008) · International Dairy Journal · doi:10.1016/j.idairyj.2007.11.009 · Cited by 289
Current Limitations and Challenges with Lactic Acid Bacteria: A Review
Hayek, S. A., & Ibrahim, S. A. (2013) · Food and Nutrition Sciences · doi:10.4236/fns.2013.411a010 · Cited by 277
Bacteriocins: Recent trends and potential applications
Bali, V., Panesar, P. S., Bera, M. B., & Kennedy, J. F. (2016) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2012.729231 · Cited by 119
Metadata
- Authors
- Cintas, L. M., Casaus, M. P., Herranz, C., Nes, I. F., & Hernández, P. E.
- Venue
- Food Science and Technology International
- Publisher
- SAGE Publications
- Published
- 2001-08
- Volume
- 7
- Issue
- 4
- Pages
- 281-305
- ISSN
- 1082-0132 (ISSN-L)
- 1532-1738
- OpenAlex
- W1985485191
- Cited by
- 318
- References
- 208
- FWCI
- 4.04
- Type
- journal article
- Language
- en
- Open access
- closed
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