Evidence map›Paper›PMID 27114507›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

MIB-MIP is a mycoplasma system that captures and cleaves immunoglobulin G.

Yonathan Arfi, Laetitia Minder, Carmelo Di Primo, Aline Le Roy, Christine Ebel, Laurent Coquet, Stephane Claverol, Sanjay Vashee, Joerg Jores, Alain Blanchard and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
5.6field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

60 citing papers in PubMed, 89 citations in OpenAlex.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

11 authors at 8 institutions in 4 countries.

Yonathan ArfiINRA (Institut National de la Recherche Agronomique), UMR 1332 Biologie du Fruit et Pathologie, F-33882 Villenave d'Ornon, France; University of Bordeaux, UMR 1332 Biologie du Fruit et Pathologie, F-33882 Villenave d'Ornon, France; yonathan.arfi@u-bordeaux.fr.
Laetitia MinderInstitut Européen de Chimie et Biologie, UMS 3033, University of Bordeaux, 33607 Pessac, France; Institut Bergonié, SIRIC BRIO, 33076 Bordeaux, France;
Carmelo Di PrimoINSERM U1212, ARN Regulation Naturelle et Artificielle, 33607 Pessac, France; CNRS UMR 5320, ARN Regulation Naturelle et Artificielle, 33607 Pessac, France; Institut Européen de Chimie et Biologie, University of Bordeaux, 33607 Pessac, France;
Aline Le RoyInstitut de Biologie Structurale, University of Grenoble Alpes, F-38044 Grenoble, France; CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France; CEA, Institut de Biologie Structurale, F-38044 Grenoble, France;
Christine EbelInstitut de Biologie Structurale, University of Grenoble Alpes, F-38044 Grenoble, France; CNRS, Institut de Biologie Structurale, F-38044 Grenoble, France; CEA, Institut de Biologie Structurale, F-38044 Grenoble, France;
Laurent CoquetCNRS UMR 6270, Plateforme PISSARO, Institute for Research and Innovation in Biomedicine - Normandie Rouen, Normandie Université, F-76821 Mont-Saint-Aignan, France;
Stephane ClaverolProteome Platform, Functional Genomic Center of Bordeaux, University of Bordeaux, F-33076 Bordeaux Cedex, France;
Sanjay VasheeJ. Craig Venter Institute, Rockville, MD 20850;
Joerg JoresInternational Livestock Research Institute, 00100 Nairobi, Kenya; Institute of Veterinary Bacteriology, University of Bern, CH-3001 Bern, Switzerland.
Alain BlanchardINRA (Institut National de la Recherche Agronomique), UMR 1332 Biologie du Fruit et Pathologie, F-33882 Villenave d'Ornon, France; University of Bordeaux, UMR 1332 Biologie du Fruit et Pathologie, F-33882 Villenave d'Ornon, France;
Pascal Sirand-PugnetINRA (Institut National de la Recherche Agronomique), UMR 1332 Biologie du Fruit et Pathologie, F-33882 Villenave d'Ornon, France; University of Bordeaux, UMR 1332 Biologie du Fruit et Pathologie, F-33882 Villenave d'Ornon, France;
Biologie du Fruit et Pathologie · FRCentre National de la Recherche Scientifique · FRUniversité de Bordeaux · FRCEA Grenoble · FRInstitut Bergonié · FRJ. Craig Venter Institute · USNormandie Université · FRUniversity of Bern · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mycoplasmas 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.

Indexed as

Bacterial ProteinsImmunoglobulin GMultiprotein ComplexesMycoplasma mycoidesProtein BindingBacterial ProteinsImmunoglobulin GMultiprotein Complexesimmunoglobulinmycoplasmasprotease

Identifiers

PMID27114507
PMCPMC4868467
OpenAlexW2345026474

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.