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<title lang=en>Proteomic studies highlight outer-membrane proteins related to biofilm development in the marine bacterium Pseudoalteromonas sp. D41</title>
<creator>Ritter, Andrés</creator>
<creator>Com, Emmanuelle</creator>
<creator>Bazire, Alexis</creator>
<creator>Goncalves Dos Santos, Marina</creator>
<creator>Delage, Ludovic</creator>
<creator>Le Pennec, Gaël</creator>
<creator>Pineau, Charles</creator>
<creator>Dreanno, Catherine</creator>
<creator>Compère, Chantal</creator>
<creator>Dufour, Alain</creator>
<contributor>Service Interfaces et Capteurs (IFREMER) ; Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)</contributor>
<contributor>Plateforme Protéomique-Biogenouest (PPB) ; Institut de recherche, santé, environnement et travail [Rennes] (Irset) ; Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Université d'Angers (UA) - Université des Antilles et de la Guyane (UAG) - Université de Rennes 1 (UR1) - École des Hautes Études en Santé Publique [EHESP] (EHESP) - Institut National de la Santé et de la Recherche Médicale (INSERM) - Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ) - Proteomics Core Facility (Protim) ; Université de Rennes 1 (UR1) - Plateforme Génomique Santé Biogenouest® - Plateforme Génomique Santé Biogenouest®</contributor>
<contributor>Laboratoire de Biotechnologie et Chimie Marines (LBCM) ; Université de Bretagne Sud (UBS) - Université de Brest (UBO)</contributor>
<description>International audience</description>
<source>ISSN: 1615-9853</source>
<source>EISSN: 1615-9861</source>
<source>Proteomics</source>
<publisher>Wiley-VCH Verlag</publisher>
<identifier>hal-00864093</identifier>
<identifier>https://hal.archives-ouvertes.fr/hal-00864093</identifier>
<source>https://hal.archives-ouvertes.fr/hal-00864093</source>
<source>Proteomics, Wiley-VCH Verlag, 2012, 12 (21), pp.3180-3192. 〈10.1002/pmic.201100644〉</source>
<identifier>DOI : 10.1002/pmic.201100644</identifier>
<relation>info:eu-repo/semantics/altIdentifier/doi/10.1002/pmic.201100644</relation>
<language>en</language>
<subject>[SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology</subject>
<type>info:eu-repo/semantics/article</type>
<type>Journal articles</type>
<description lang=en>Bacterial biofilm development is conditioned by complex processes involving bacterial attachment to surfaces, growth, mobility, and exoproduct production. The marine bacterium Pseudoalteromonas sp. strain D41 is able to attach strongly onto a wide variety of substrates, which promotes subsequent biofilm development. Study of the outer-membrane and total soluble proteomes showed ten spots with significant intensity variations when this bacterium was grown in biofilm compared to planktonic cultures. MS/MS de novo sequencing analysis allowed the identification of four outer-membrane proteins of particular interest since they were strongly induced in biofilms. These proteins are homologous to a TonB-dependent receptor (TBDR), to the OmpW and OmpA porins, and to a type IV pilus biogenesis protein (PilF). Gene expression assays by quantitative RT-PCR showed that the four corresponding genes were upregulated during biofilm development on hydrophobic and hydrophilic surfaces. The Pseudomonas aeruginosa mutants unable to produce any of the OmpW, OmpA, and PilF homologues yielded biofilms with lower biovolumes and altered architectures, confirming the involvement of these proteins in the biofilm formation process. Our results indicate that Pseudoalteromonas sp. D41 shares biofilm formation mechanisms with human pathogenic bacteria, but also relies on TBDR, which might be more specific to the marine environment.</description>
<date>2012</date>
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