|Entry||Database: EMDB / ID: EMD-11731|
|Title||CryoEM structure of MIB in complex with a polyclonal goat Fab|
|Sample||Mycoplasma MIB protein in complex with a goat Fab|
|Function / homology||Mycoplasma virulence, signal domain / Putative immunoglobulin-blocking virulence protein / IgG-blocking virulence domain / Putative immunoglobulin-blocking virulence protein|
Function and homology information
|Biological species||Mycoplasma mycoides subsp. capri str. GM12 (bacteria) / Mycoplasma mycoides subsp. capri (bacteria)|
|Method||single particle reconstruction / cryo EM / Resolution: 3.5 Å|
|Authors||Nottelet P / Bataille L / Gourgues G / Anger R / Lartigue C / Sirand-Pugnet P / Marza E / Fronzes R / Arfi Y|
|Funding support|| France, 1 items |
|Citation||Journal: Sci Adv / Year: 2021|
Title: The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction.
Authors: Pierre Nottelet / Laure Bataille / Geraldine Gourgues / Robin Anger / Carole Lartigue / Pascal Sirand-Pugnet / Esther Marza / Remi Fronzes / Yonathan Arfi /
Abstract: Mycoplasma immunoglobulin binding (MIB) and mycoplasma immunoglobulin protease (MIP) are surface proteins found in the majority of mycoplasma species, acting sequentially to capture antibodies and ...Mycoplasma immunoglobulin binding (MIB) and mycoplasma immunoglobulin protease (MIP) are surface proteins found in the majority of mycoplasma species, acting sequentially to capture antibodies and cleave off their V domains. Cryo-electron microscopy structures show how MIB and MIP bind to a Fab fragment in a "hug of death" mechanism. As a result, the orientation of the V and V domains is twisted out of alignment, disrupting the antigen binding site. We also show that MIB-MIP has the ability to promote the dissociation of the antibody-antigen complex. This system is functional in cells and protects mycoplasmas from antibody-mediated agglutination. These results highlight the key role of the MIB-MIP system in immunity evasion by mycoplasmas through an unprecedented mechanism, and open exciting perspectives to use these proteins as potential tools in the antibody field.
|Validation Report||Summary, Full report, XML, About validation report|
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_11731.map.gz / Format: CCP4 / Size: 15.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.13 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Additional map: #1
|Projections & Slices|
-Half map: #1
|Projections & Slices|
-Half map: #2
-Entire Mycoplasma MIB protein in complex with a goat Fab
|Entire||Name: Mycoplasma MIB protein in complex with a goat Fab / Number of components: 2|
-Component #1: protein, Mycoplasma MIB protein in complex with a goat Fab
|Protein||Name: Mycoplasma MIB protein in complex with a goat Fab / Recombinant expression: No|
|Source||Species: Mycoplasma mycoides subsp. capri str. GM12 (bacteria)|
|Source (engineered)||Expression System: Escherichia coli BL21(DE3) (bacteria) / Strain: Rosetta|
-Component #2: protein, Putative immunoglobulin-blocking virulence protein
|Protein||Name: Putative immunoglobulin-blocking virulence protein / Number of Copies: 1 / Recombinant expression: No|
|Mass||Theoretical: 84.962719 kDa|
|Source||Species: Mycoplasma mycoides subsp. capri (bacteria)|
|Source (engineered)||Expression System: Escherichia coli BL21(DE3) (bacteria)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||pH: 8|
|Vitrification||Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Temperature: 4 K / Humidity: 100 %|
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Imaging||Microscope: FEI TALOS ARCTICA|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 0.77 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Cs: 2.7 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: GATAN K2 SUMMIT (4k x 4k)|
|Processing||Method: single particle reconstruction / Number of projections: 3517059|
|3D reconstruction||Software: cryoSPARC / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF|
-Atomic model buiding
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