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hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorARFI, Yonathan
hal.structure.identifierInstitut Européen de Chimie et de Biologie
dc.contributor.authorMINDER, Laetitia
hal.structure.identifierInstitut Européen de Chimie et de Biologie
dc.contributor.authorDI PRIMO, Carmelo
hal.structure.identifierInstitut de biologie structurale [IBS - UMR 5075 ]
dc.contributor.authorLE ROY, Aline
hal.structure.identifierInstitut de biologie structurale [IBS - UMR 5075 ]
dc.contributor.authorEBEL, Christine
hal.structure.identifierPolymères Biopolymères Surfaces [PBS]
dc.contributor.authorCOQUET, Laurent
hal.structure.identifierCentre Génomique Fonctionnelle Bordeaux [Bordeaux] [CGFB]
dc.contributor.authorCLAVEROL, Stephane
hal.structure.identifierJ. Craig Venter Institute
dc.contributor.authorVASHEE, Sanjay
hal.structure.identifierInternational Livestock Research Institute
dc.contributor.authorJORES, Joerg
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorBLANCHARD, Alain
hal.structure.identifierBiologie du fruit et pathologie [BFP]
dc.contributor.authorSIRAND-PUGNET, Pascal
dc.date.issued2016-05-10
dc.identifier.issn0027-8424
dc.description.abstractEnMycoplasmas are "minimal" bacteria able to infect humans, wildlife, and a large number of economically important livestock species. Mycoplasma infections include a spectrum of clinical manifestations ranging from simple fever to fulminant inflammatory diseases with high mortality rates. These infections are mostly chronic, suggesting that mycoplasmas have developed means to evade the host immune response. Here we present and functionally characterize a two-protein system from Mycoplasma mycoides subspecies capri that is involved in the capture and cleavage of IgG. The first component, Mycoplasma Ig binding protein (MIB), is an 83-kDa protein that is able to tightly bind to the Fv region of a wide range of IgG. The second component, Mycoplasma Ig protease (MIP), is a 97-kDa serine protease that is able to cleave off the VH domain of IgG. We demonstrate that MIB is necessary for the proteolytic activity of MIP. Cleavage of IgG requires a sequential interaction of the different partners of the system: first MIB captures the IgG, and then MIP is recruited to the MIB-IgG complex, enabling protease activity. MIB and MIP are encoded by two genes organized in tandem, with homologs found in the majority of pathogenic mycoplasmas and often in multiple copies. Phylogenetic studies suggest that genes encoding the MIB-MIP system are specific to mycoplasmas and have been disseminated by horizontal gene transfer. These results highlight an original and complex system targeting the host immunoglobulins, playing a potentially key role in the immunity evasion by mycoplasmas.
dc.language.isoen
dc.publisherNational Academy of Sciences
dc.subjectimmunoglobulin
dc.subject.enmycoplasmas
dc.subject.enprotease
dc.title.enMIB-MIP is a mycoplasma system that captures and cleaves immunoglobulin G.
dc.typeArticle de revue
dc.identifier.doi10.1073/pnas.1600546113
dc.subject.halSciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire/Biologie structurale [q-bio.BM]
bordeaux.journalProceedings of the National Academy of Sciences of the United States of America
bordeaux.page5406-11
bordeaux.volume113
bordeaux.issue19
bordeaux.peerReviewedoui
hal.identifierhal-01327385
hal.version1
hal.popularnon
hal.audienceInternationale
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-01327385v1
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