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The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction
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(H) domains. Cryo–electron microscopy structures show how MIB and MIP bind to a Fab f...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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American Association for the Advancement of Science
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7935358/ https://www.ncbi.nlm.nih.gov/pubmed/33674316 http://dx.doi.org/10.1126/sciadv.abf2403 |
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author | Nottelet, Pierre Bataille, Laure Gourgues, Geraldine Anger, Robin Lartigue, Carole Sirand-Pugnet, Pascal Marza, Esther Fronzes, Remi Arfi, Yonathan |
author_facet | Nottelet, Pierre Bataille, Laure Gourgues, Geraldine Anger, Robin Lartigue, Carole Sirand-Pugnet, Pascal Marza, Esther Fronzes, Remi Arfi, Yonathan |
author_sort | Nottelet, Pierre |
collection | PubMed |
description | 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(H) 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(L) and V(H) 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. |
format | Online Article Text |
id | pubmed-7935358 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | American Association for the Advancement of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-79353582021-03-17 The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction Nottelet, Pierre Bataille, Laure Gourgues, Geraldine Anger, Robin Lartigue, Carole Sirand-Pugnet, Pascal Marza, Esther Fronzes, Remi Arfi, Yonathan Sci Adv Research Articles 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(H) 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(L) and V(H) 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. American Association for the Advancement of Science 2021-03-05 /pmc/articles/PMC7935358/ /pubmed/33674316 http://dx.doi.org/10.1126/sciadv.abf2403 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC). https://creativecommons.org/licenses/by-nc/4.0/ https://creativecommons.org/licenses/by-nc/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial license (https://creativecommons.org/licenses/by-nc/4.0/) , which permits use, distribution, and reproduction in any medium, so long as the resultant use is not for commercial advantage and provided the original work is properly cited. |
spellingShingle | Research Articles Nottelet, Pierre Bataille, Laure Gourgues, Geraldine Anger, Robin Lartigue, Carole Sirand-Pugnet, Pascal Marza, Esther Fronzes, Remi Arfi, Yonathan The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction |
title | The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction |
title_full | The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction |
title_fullStr | The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction |
title_full_unstemmed | The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction |
title_short | The mycoplasma surface proteins MIB and MIP promote the dissociation of the antibody-antigen interaction |
title_sort | mycoplasma surface proteins mib and mip promote the dissociation of the antibody-antigen interaction |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7935358/ https://www.ncbi.nlm.nih.gov/pubmed/33674316 http://dx.doi.org/10.1126/sciadv.abf2403 |
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