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-Structure paper
Title | The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction. |
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Journal, issue, pages | Sci Adv, Vol. 7, Issue 10, Year 2021 |
Publish date | Mar 5, 2021 |
Authors | Pierre Nottelet / Laure Bataille / Geraldine Gourgues / Robin Anger / Carole Lartigue / Pascal Sirand-Pugnet / Esther Marza / Remi Fronzes / Yonathan Arfi / |
PubMed 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. |
External links | Sci Adv / PubMed:33674316 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.8 - 3.5 Å |
Structure data | EMDB-11727: Cryo-EM structure of the mycoplasma MIB-MIP proteins in complex with a goat Fab EMDB-11729: CryoEM structure of MIB-MIP in complex with a polyclonal goat Fab EMDB-11731: CryoEM structure of MIB in complex with a polyclonal goat Fab |
Source |
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Keywords | MEMBRANE PROTEIN / Antibody binding protein / protease / protein complex. |