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Título: | Isolation of Lactococcus lactis mutants simultaneously resistant to the cell wall-active bacteriocin Lcn972, lysozyme, nisin, and bacteriophage c2 |
Autor: | Roces, Clara CSIC ORCID; Courtin, Pascal; Kulakauskas, Saulius; Rodríguez González, Ana CSIC ORCID; Chapot-Chartier, Marie-Pierre; Martínez Fernández, Beatriz CSIC ORCID | Fecha de publicación: | 2012 | Editor: | American Society for Microbiology | Citación: | Applied and Environmental Microbiology 78(12): 4157-4163 (2012) | Resumen: | Lactococcin 972 (Lcn972) is a nonlantibiotic bacteriocin that inhibits cell wall biosynthesis by binding to lipid II. In this work, two mutants resistant to Lcn972, Lactococcus lactis D1 and D1-20, with high (>320 arbitrary units [AU]/ml) and low (80 AU/ml) susceptibilities, respectively, have been isolated. Resistance to Lcn972 did not impose a burden to growth under laboratory conditions, nor did it substantially alter the physicochemical properties of the cell surface. However, the peptidoglycan of the mutants featured a higher content of muropeptides with tripeptide side chains than the wild-type strain, linking for the first time peptidoglycan remodelling to bacteriocin resistance. Moreover, L. lactis lacking a functional D, D-carboxypeptidase DacA (i.e., with a high content of pentapeptide side chain muropeptides) was shown to be more susceptible to Lcn972. Cross-resistance to lysozyme and nisin and enhanced susceptibility to penicillin G and bacitracin was also observed. Intriguingly, the Lcn972-resistant mutants were not infected by the lytic phage c2 and less efficiently infected by phage sk1. Lack of c2 infectivity was linked to a 22.6-kbp chromosomal deletion encompassing the phage receptor protein gene pip. The deletion also included maltose metabolic genes and the two-component system (TCS) F. However, a clear correlation between these genes and resistance to Lcn972 could not be clearly established, pointing to the presence of as-yet-unidentified mutations that account for Lcn972 resistance. © 2012, American Society for Microbiology. | Descripción: | Este artículo forma parte de la tesis de clara Roces. Mecanismos moleculares de respuesta al estrés sobre la pared celular en Lactococcus lactis. http://hdl.handle.net/10261/109851 | Versión del editor: | http://dx.doi.org/10.1128/AEM.00795-12 | URI: | http://hdl.handle.net/10261/81013 | DOI: | 10.1128/AEM.00795-12 | Identificadores: | doi: 10.1128/AEM.00795-12 issn: 0099-2240 e-issn: 1098-5336 |
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