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Exoproteome Analysis of Antagonistic Interactions between the Probiotic Bacteria Limosilactobacillus reuteri LR1 and Lacticaseibacillus rhamnosus F and Multidrug Resistant Strain of Klebsiella pneumonia

The expansion of multiple drug resistant (MDR) strains of presents an immense threat for public health. Annually, this microorganism causes thousands of lethal nosocomial infections worldwide. Currently, it has been shown that certain strains of lactic acid bacteria (LAB) can efficiently inhibit gro...

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Published in:International journal of molecular sciences 2021-10, Vol.22 (20), p.10999
Main Authors: Savinova, Olga S, Glazunova, Olga A, Moiseenko, Konstantin V, Begunova, Anna V, Rozhkova, Irina V, Fedorova, Tatyana V
Format: Article
Language:English
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Summary:The expansion of multiple drug resistant (MDR) strains of presents an immense threat for public health. Annually, this microorganism causes thousands of lethal nosocomial infections worldwide. Currently, it has been shown that certain strains of lactic acid bacteria (LAB) can efficiently inhibit growth of and the formation of its biofilms; however, the active principle of such action remains unknown. In the current article, the growth inhibition of MDR by two LAB- LR1 and F-is demonstrated, and the nature of this inhibition studied at the level of exoproteome. This article shows that the exoproteomes of studied LAB contains both classically and non-classically secreted proteins. While for LR1 the substantial portion of classically secreted proteins was presented by cell-wall-degrading enzymes, for F only one out of four classically secreted proteins was presented by cell-wall hydrolase. Non-classically secreted proteins of both LAB were primarily metabolic enzymes, for some of which a possible moonlighting functioning was proposed. These results contribute to knowledge regarding antagonistic interaction between LAB and pathogenic and opportunistic microorganisms and set new perspectives for the use of LAB to control the spread of these microorganisms.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms222010999