1. Proteomic analysis and immunogenicity of secreted proteins from Rhodococcus equi ATCC 33701
- Author
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Aurélie Budin-Verneuil, Axel Hartke, Vianney Pichereau, Séverine Cauchard, Claire Laugier, Corinne Barbey, Sandrine Petry, Unité de Recherche Risques Microbiens ( U2RM ), Université de Caen Normandie ( UNICAEN ), Normandie Université ( NU ) -Normandie Université ( NU ), Laboratoire de Pathologie équine de Dozulé, ANSES, Laboratoire des Sciences de l'Environnement Marin (LEMAR) ( LEMAR ), Centre National de la Recherche Scientifique ( CNRS ) -Université de Brest ( UBO ) -Institut Français de Recherche pour l'Exploitation de la Mer ( IFREMER ) -Institut Universitaire Européen de la Mer ( IUEM ), Institut de Recherche pour le Développement ( IRD ) -Université de Brest ( UBO ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut de Recherche pour le Développement ( IRD ) -Université de Brest ( UBO ) -Centre National de la Recherche Scientifique ( CNRS ) -Institut de Recherche pour le Développement ( IRD ), Unité de Recherche Risques Microbiens (U2RM), Université de Caen Normandie (UNICAEN), Normandie Université (NU)-Normandie Université (NU), Laboratoire d'études et de recherches en pathologie équine, Agence Française de Sécurité Sanitaire des Aliments (AFSSA), Laboratoire des Sciences de l'Environnement Marin (LEMAR) (LEMAR), Institut de Recherche pour le Développement (IRD)-Institut Français de Recherche pour l'Exploitation de la Mer (IFREMER)-Université de Brest (UBO)-Institut Universitaire Européen de la Mer (IUEM), and Institut de Recherche pour le Développement (IRD)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Institut national des sciences de l'Univers (INSU - CNRS)-Université de Brest (UBO)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
- Subjects
MESH: Mycobacterium tuberculosis ,Proteome ,MESH: Sequence Homology, Amino Acid ,MESH: Trypsin ,MESH : Enzymes ,MESH: Amino Acid Sequence ,Proteomics ,Mass Spectrometry ,[ SDV.MP ] Life Sciences [q-bio]/Microbiology and Parasitology ,MESH : Actinomycetales Infections ,MESH : Bacterial Proteins ,Trypsin ,MESH: Animals ,Rhodococcus equi ,MESH: Bacterial Proteins ,MESH : Temperature ,Peptide sequence ,MESH : Immunoblotting ,0303 health sciences ,MESH: Immunoblotting ,MESH : Horse Diseases ,MESH : Amino Acid Sequence ,Immunogenicity ,MESH : Antigens, Bacterial ,Temperature ,General Medicine ,MESH: Temperature ,MESH : Sequence Homology, Amino Acid ,Enzymes ,3. Good health ,MESH: Proteome ,[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology ,Electrophoresis, Polyacrylamide Gel ,MESH : DNA Primers ,Actinomycetales Infections ,MESH: DNA Primers ,Signal peptide ,MESH: Rhodococcus equi ,Sequence analysis ,Immunoblotting ,MESH: Enzymes ,MESH : Proteome ,Biology ,MESH : Electrophoresis, Polyacrylamide Gel ,Microbiology ,MESH : Mycobacterium tuberculosis ,03 medical and health sciences ,MESH : Mass Spectrometry ,Bacterial Proteins ,Animals ,Amino Acid Sequence ,Horses ,MESH: Horses ,DNA Primers ,030304 developmental biology ,MESH: Mass Spectrometry ,Antigens, Bacterial ,Sequence Homology, Amino Acid ,General Veterinary ,MESH : Rhodococcus equi ,030306 microbiology ,Mycobacterium tuberculosis ,biology.organism_classification ,Secretory protein ,MESH : Horses ,Horse Diseases ,MESH : Trypsin ,MESH : Animals ,MESH: Horse Diseases ,MESH: Antigens, Bacterial ,MESH: Actinomycetales Infections ,MESH: Electrophoresis, Polyacrylamide Gel - Abstract
International audience; Rhodococcus equi is one of the most important causes of mortality in foals between 1 and 6 months of age. Although rare, infection also occurs in a variety of other mammals including humans, often following immunosuppression of various causes. Secreted proteins are known to mediate important pathogen-host interactions and consequently are favored candidates for vaccine development as they are the most easily accessible microbial antigens to the immune system. Here, we describe the results of a proteomic analysis based on SDS-PAGE, immunoblot and mass spectrometry, which was carried out aiming the identification of secreted proteins that are differently expressed at 30 degrees C versus 37 degrees C and at mid-exponential versus early-stationary growth phase and antigenic proteins from R. equi ATCC 33701. A total of 48 proteins was identified regardless of growth conditions. The cholesterol oxidase ChoE appears to be the major secretory protein. Moreover, four proteins revealed high homologies with the mycolyl transferases of the Ag85 complex from Mycobacterium tuberculosis. The sequence analysis predicted that 24 proteins are transported by a signal peptide-dependent pathway. Moreover, five antigenic proteins of R. equi were identified by immunoblot, including a novel strongly immunoreactive protein of unknown function. In conclusion, the elucidation of the secretome of R. equi identified several proteins with different biological functions and a new candidate for developing vaccines against R. equi infection in horse.
- Published
- 2009
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