Academic Journal
Membrane proteocomplexome of Campylobacter jejuni using 2-D blue native/SDS-PAGE combined to bioinformatics analysis
| العنوان: | Membrane proteocomplexome of Campylobacter jejuni using 2-D blue native/SDS-PAGE combined to bioinformatics analysis |
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| المؤلفون: | Guérin, Alizée, Sulaeman, Sheiam, Coquet, Laurent, Ménard, Armelle, Barloy-Hubler, Frédérique, Dé, Emmanuelle, Tresse, Odile |
| المساهمون: | SECurité des ALIments et Microbiologie (SECALIM), École nationale vétérinaire, agroalimentaire et de l'alimentation Nantes-Atlantique (ONIRIS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Polymères Biopolymères Surfaces (PBS), Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut Normand de Chimie Moléculaire Médicinale et Macromoléculaire (INC3M), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Université Le Havre Normandie (ULH), Normandie Université (NU)-Université de Rouen Normandie (UNIROUEN), Normandie Université (NU)-Institut national des sciences appliquées Rouen Normandie (INSA Rouen Normandie), Institut National des Sciences Appliquées (INSA)-Normandie Université (NU)-Institut National des Sciences Appliquées (INSA)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Université de Caen Normandie (UNICAEN), Normandie Université (NU)-École Nationale Supérieure d'Ingénieurs de Caen (ENSICAEN), Normandie Université (NU)-Institut de Chimie - CNRS Chimie (INC-CNRS)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), UNIROUEN - UFR Santé (UNIROUEN UFR Santé), Normandie Université (NU)-Normandie Université (NU), Bordeaux Research In Translational Oncology Bordeaux (BaRITOn), Université de Bordeaux (UB)-CHU Bordeaux-Institut National de la Santé et de la Recherche Médicale (INSERM), Institut de Génétique et Développement de Rennes (IGDR), Université de Rennes (UR)-Centre National de la Recherche Scientifique (CNRS)-Structure Fédérative de Recherche en Biologie et Santé de Rennes ( Biosit : Biologie - Santé - Innovation Technologique ), Institut National de la Recherche Agronomique |
| المصدر: | ISSN: 1664-302X. |
| بيانات النشر: | HAL CCSD Frontiers Media |
| سنة النشر: | 2020 |
| المجموعة: | Université de Rennes 1: Publications scientifiques (HAL) |
| مصطلحات موضوعية: | blue native electrophoresis, complexes, efflux pumps, foodborne pathogen, functional genomics, membrane proteins, proteomics, regulation, [SDV.AEN]Life Sciences [q-bio]/Food and Nutrition |
| الوصف: | International audience ; Campylobacter is the leading cause of the human bacterial foodborne infections in the developed countries. The perception cues from biotic or abiotic environments by the bacteria are often related to bacterial surface and membrane proteins that mediate the cellular response for the adaptation of Campylobacter jejuni to the environment. These proteins function rarely as a unique entity, they are often organized in functional complexes. In C. jejuni , these complexes are not fully identified and some of them remain unknown. To identify putative functional multi-subunit entities at the membrane subproteome level of C. jejuni , a holistic non a priori method was addressed using two-dimensional blue native/Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) in strain C. jejuni 81–176. Couples of acrylamide gradient/migration-time, membrane detergent concentration and hand-made strips were optimized to obtain reproducible extraction and separation of intact membrane protein complexes (MPCs). The MPCs were subsequently denatured using SDS-PAGE and each spot from each MPCs was identified by mass spectrometry. Altogether, 21 MPCs could be detected including multi homo-oligomeric and multi hetero-oligomeric complexes distributed in both inner and outer membranes. The function, the conservation and the regulation of the MPCs across C. jejuni strains were inspected by functional and genomic comparison analyses. In this study, relatedness between subunits of two efflux pumps, CmeABC and MacABputC was observed. In addition, a consensus sequence CosR-binding box in promoter regions of MacABputC was present in C. jejuni but not in Campylobacter coli . The MPCs identified in C. jejuni 81–176 membrane are involved in protein folding, molecule trafficking, oxidative phosphorylation, membrane structuration, peptidoglycan biosynthesis, motility and chemotaxis, stress signaling, efflux pumps and virulence. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | English |
| Relation: | info:eu-repo/semantics/altIdentifier/pmid/33329413; hal-03765916; https://hal.inrae.fr/hal-03765916; https://hal.inrae.fr/hal-03765916/document; https://hal.inrae.fr/hal-03765916/file/530906_Manuscript.PDF; PUBMED: 33329413; WOS: 000595126600001 |
| DOI: | 10.3389/fmicb.2020.530906 |
| الاتاحة: | https://hal.inrae.fr/hal-03765916 https://hal.inrae.fr/hal-03765916/document https://hal.inrae.fr/hal-03765916/file/530906_Manuscript.PDF https://doi.org/10.3389/fmicb.2020.530906 |
| Rights: | http://creativecommons.org/licenses/by/ ; info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: | edsbas.F6DC5FE0 |
| قاعدة البيانات: | BASE |
| DOI: | 10.3389/fmicb.2020.530906 |
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