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The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets

Staphylococcus epidermidis is a bacterium frequently isolated from contaminated platelet concentrates (PCs), a blood product used to treat bleeding disorders in transfusion patients. PCs offer an accidental niche for colonization of S. epidermidis by forming biofilms and thus avoiding clearance by i...

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Autores principales: Loza-Correa, Maria, Ayala, Juan A., Perelman, Iris, Hubbard, Keith, Kalab, Miloslav, Yi, Qi-Long, Taha, Mariam, de Pedro, Miguel A., Ramirez-Arcos, Sandra
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6347161/
https://www.ncbi.nlm.nih.gov/pubmed/30682094
http://dx.doi.org/10.1371/journal.pone.0211132
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author Loza-Correa, Maria
Ayala, Juan A.
Perelman, Iris
Hubbard, Keith
Kalab, Miloslav
Yi, Qi-Long
Taha, Mariam
de Pedro, Miguel A.
Ramirez-Arcos, Sandra
author_facet Loza-Correa, Maria
Ayala, Juan A.
Perelman, Iris
Hubbard, Keith
Kalab, Miloslav
Yi, Qi-Long
Taha, Mariam
de Pedro, Miguel A.
Ramirez-Arcos, Sandra
author_sort Loza-Correa, Maria
collection PubMed
description Staphylococcus epidermidis is a bacterium frequently isolated from contaminated platelet concentrates (PCs), a blood product used to treat bleeding disorders in transfusion patients. PCs offer an accidental niche for colonization of S. epidermidis by forming biofilms and thus avoiding clearance by immune factors present in this milieu. Using biochemical and microscopy techniques, we investigated the structural changes of the peptidoglycan (PG) and the biofilm matrix of S. epidermidis biofilms formed in whole-blood derived PCs compared to biofilms grown in glucose-supplemented trypticase soy broth (TSBg). Both, the PG and the biofilm matrix are primary mechanisms of defense against environmental stress. Here we show that in PCs, the S. epidermidis biofilm matrix is mainly of a proteinaceous nature with extracellular DNA, in contrast to the predominant polysaccharide nature of the biofilm matrix formed in TSBg cultures. PG profile studies demonstrated that the PG of biofilm cells remodels during PC storage displaying fewer muropeptides variants than those observed in TSBg. The PG muropeptides contain two chemical modifications (amidation and O-acetylation) previously associated with resistance to antimicrobial agents by other staphylococci. Our study highlights two key structural features of S. epidermidis that are remodeled when exposed to human platelets and could be used as targets to reduce septic transfusions events.
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spelling pubmed-63471612019-02-02 The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets Loza-Correa, Maria Ayala, Juan A. Perelman, Iris Hubbard, Keith Kalab, Miloslav Yi, Qi-Long Taha, Mariam de Pedro, Miguel A. Ramirez-Arcos, Sandra PLoS One Research Article Staphylococcus epidermidis is a bacterium frequently isolated from contaminated platelet concentrates (PCs), a blood product used to treat bleeding disorders in transfusion patients. PCs offer an accidental niche for colonization of S. epidermidis by forming biofilms and thus avoiding clearance by immune factors present in this milieu. Using biochemical and microscopy techniques, we investigated the structural changes of the peptidoglycan (PG) and the biofilm matrix of S. epidermidis biofilms formed in whole-blood derived PCs compared to biofilms grown in glucose-supplemented trypticase soy broth (TSBg). Both, the PG and the biofilm matrix are primary mechanisms of defense against environmental stress. Here we show that in PCs, the S. epidermidis biofilm matrix is mainly of a proteinaceous nature with extracellular DNA, in contrast to the predominant polysaccharide nature of the biofilm matrix formed in TSBg cultures. PG profile studies demonstrated that the PG of biofilm cells remodels during PC storage displaying fewer muropeptides variants than those observed in TSBg. The PG muropeptides contain two chemical modifications (amidation and O-acetylation) previously associated with resistance to antimicrobial agents by other staphylococci. Our study highlights two key structural features of S. epidermidis that are remodeled when exposed to human platelets and could be used as targets to reduce septic transfusions events. Public Library of Science 2019-01-25 /pmc/articles/PMC6347161/ /pubmed/30682094 http://dx.doi.org/10.1371/journal.pone.0211132 Text en © 2019 Loza-Correa et al http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
spellingShingle Research Article
Loza-Correa, Maria
Ayala, Juan A.
Perelman, Iris
Hubbard, Keith
Kalab, Miloslav
Yi, Qi-Long
Taha, Mariam
de Pedro, Miguel A.
Ramirez-Arcos, Sandra
The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets
title The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets
title_full The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets
title_fullStr The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets
title_full_unstemmed The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets
title_short The peptidoglycan and biofilm matrix of Staphylococcus epidermidis undergo structural changes when exposed to human platelets
title_sort peptidoglycan and biofilm matrix of staphylococcus epidermidis undergo structural changes when exposed to human platelets
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6347161/
https://www.ncbi.nlm.nih.gov/pubmed/30682094
http://dx.doi.org/10.1371/journal.pone.0211132
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