Impairment of the class IIa bacteriocin receptor function and membrane structural changes are associated to enterocin CRL35 high resistance in Listeria monocytogenes
| Autor: | Carlos Minahk, Emilse Masias, Juan V. Farizano, Eduardo Maffud Cilli, Paulo R. S. Sanches, Lucila Saavedra, Augusto Bellomio, Fernando Gabriel Dupuy |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Receptor expression Membrane lipids Otras Ciencias Biológicas 030106 microbiology Biophysics Microbial Sensitivity Tests Biology medicine.disease_cause Biochemistry Microbiology Cell wall Ciencias Biológicas 03 medical and health sciences Membrane Lipids Listeria monocytogenes Bacteriocin Bacteriocins SYNTHETIC PEPTIDES Drug Resistance Bacterial medicine Molecular Biology Cell Membrane Glucose transporter food and beverages biology.organism_classification BACTERIOCINS ENTEROCIN CRL35 Membrane Glucose Listeria CIENCIAS NATURALES Y EXACTAS LISTERIA |
| Zdroj: | Biochimica et biophysica acta. General subjects. 1861(7) |
| ISSN: | 0304-4165 |
| Popis: | Background: Enterocin CRL35 is a class IIa bacteriocin with anti-Listeria activity. Resistance to these peptides has been associated with either the downregulation of the receptor expression or changes in the membrane and cell walls. The scope of the present work was to characterize enterocin CRL35 resistant Listeria strains with MICs more than 10,000 times higher than the MIC of the WT sensitive strain. Methods: Listeria monocytogenes INS7 resistant isolates R2 and R3 were characterized by 16S RNA gene sequencing and rep-PCR. Bacterial growth kinetic was studied in different culture media. Plasma membranes of sensitive and resistant bacteria were characterized by FTIR and Langmuir monolayer techniques. Results: The growth kinetic of the resistant isolates was slower as compared to the parental strain in TSB medium. Moreover, the resistant isolates barely grew in a glucose-based synthetic medium, suggesting that these cells had a major alteration in glucose transport. Resistant bacteria also had alterations in their cell wall and, most importantly, membrane lipids. In fact, even though enterocin CRL35 was able to bind to the membrane-water interface of both resistant and parental sensitive strains, this peptide was only able to get inserted into the latter membranes. Conclusions: These results indicate that bacteriocin receptor is altered in combination with membrane structural modifications in enterocin CRL35-resistant L. monocytogenes strains. General significance: Highly enterocin CRL35-resistant isolates derived from Listeria monocytogenes INS7 have not only an impaired glucose transport but also display structural changes in the hydrophobic core of their plasma membranes. Fil: Masias, Ruth Emilse. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Dupuy, Fernando Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: da Silva Sanches, Paulo Ricardo. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil Fil: Farizano, Juan Vicente. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Cilli, Eduardo. Universidade Estadual Paulista Julio de Mesquita Filho; Brasil Fil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Saavedra, Maria Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucuman. Centro de Referencia Para Lactobacilos; Argentina Fil: Minahk, Carlos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina |
| Databáze: | OpenAIRE |
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