Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes

Abstract Candida albicans mannan consists of a large repertoire of oligomannosides with different types of mannose linkages and chain lengths, which act as individual epitopes with more or less overlapping antibody specificities. Although anti-C. albicans mannan antibody levels are monitored for dia...

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Autores principales:	Boualem Sendid, Karine Lecointe, Mayeul Collot, Pierre-Marie Danzé, Sébastien Damiens, Anne-Sophie Drucbert, Chantal Fradin, Jean-Pierre Vilcot, Frédéric Grenouillet, Faustine Dubar, Jérôme de Ruyck, Samir Jawhara, Jean-Maurice Mallet, Daniel Poulain
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/4979b619fcb54a9b87828257c4e0f296
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spelling	oai:doaj.org-article:4979b619fcb54a9b87828257c4e0f2962021-12-02T15:49:53ZDissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes10.1038/s41598-021-90402-42045-2322https://doaj.org/article/4979b619fcb54a9b87828257c4e0f2962021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90402-4https://doaj.org/toc/2045-2322Abstract Candida albicans mannan consists of a large repertoire of oligomannosides with different types of mannose linkages and chain lengths, which act as individual epitopes with more or less overlapping antibody specificities. Although anti-C. albicans mannan antibody levels are monitored for diagnostic purposes nothing is known about the qualitative distribution of these antibodies in terms of epitope specificity. We addressed this question using a bank of previously synthesized biotin sulfone tagged oligomannosides (BSTOs) of α and β anomery complemented with a synthetic β-mannotriose described as a protective epitope. The reactivity of these BSTOs was analyzed with IgM isotype monoclonal antibodies (MAbs) of known specificity, polyclonal sera from patients colonized or infected with C. albicans, and mannose binding lectin (MBL). Surface plasmon resonance (SPR) and multiple analyte profiling (MAP) were used. Both methods confirmed the usual reactivity of MAbs against either α or β linkages, excepted for MAb B6.1 (protective epitope) reacting with β-Man whereas the corresponding BSTO reacted with anti-α-Man. These results were confirmed in western blots with native C. albicans antigens. Using patients’ sera in MAP, a significant correlation was observed between the detection of anti-mannan antibodies recognizing β- and α-Man epitopes and detection of antibodies against β-linked mannotriose suggesting that this epitope also reacts with human polyclonal antibodies of both specificities. By contrast, the reactivity of human sera with other α- and β-linked BSTOs clearly differed according to their colonized or infected status. In these cases, the establishment of an α/β ratio was extremely discriminant. Finally SPR with MBL, an important lectin of innate immunity to C. albicans, classically known to interact with α-mannose, also interacted in an unexpected way with the protective epitope. These cumulative data suggest that structure/activity investigations of the finely tuned C. albicans anti-mannose immune response are worthwhile to increase our basic knowledge and for translation in medicine.Boualem SendidKarine LecointeMayeul CollotPierre-Marie DanzéSébastien DamiensAnne-Sophie DrucbertChantal FradinJean-Pierre VilcotFrédéric GrenouilletFaustine DubarJérôme de RuyckSamir JawharaJean-Maurice MalletDaniel PoulainNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Boualem Sendid Karine Lecointe Mayeul Collot Pierre-Marie Danzé Sébastien Damiens Anne-Sophie Drucbert Chantal Fradin Jean-Pierre Vilcot Frédéric Grenouillet Faustine Dubar Jérôme de Ruyck Samir Jawhara Jean-Maurice Mallet Daniel Poulain Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes
description	Abstract Candida albicans mannan consists of a large repertoire of oligomannosides with different types of mannose linkages and chain lengths, which act as individual epitopes with more or less overlapping antibody specificities. Although anti-C. albicans mannan antibody levels are monitored for diagnostic purposes nothing is known about the qualitative distribution of these antibodies in terms of epitope specificity. We addressed this question using a bank of previously synthesized biotin sulfone tagged oligomannosides (BSTOs) of α and β anomery complemented with a synthetic β-mannotriose described as a protective epitope. The reactivity of these BSTOs was analyzed with IgM isotype monoclonal antibodies (MAbs) of known specificity, polyclonal sera from patients colonized or infected with C. albicans, and mannose binding lectin (MBL). Surface plasmon resonance (SPR) and multiple analyte profiling (MAP) were used. Both methods confirmed the usual reactivity of MAbs against either α or β linkages, excepted for MAb B6.1 (protective epitope) reacting with β-Man whereas the corresponding BSTO reacted with anti-α-Man. These results were confirmed in western blots with native C. albicans antigens. Using patients’ sera in MAP, a significant correlation was observed between the detection of anti-mannan antibodies recognizing β- and α-Man epitopes and detection of antibodies against β-linked mannotriose suggesting that this epitope also reacts with human polyclonal antibodies of both specificities. By contrast, the reactivity of human sera with other α- and β-linked BSTOs clearly differed according to their colonized or infected status. In these cases, the establishment of an α/β ratio was extremely discriminant. Finally SPR with MBL, an important lectin of innate immunity to C. albicans, classically known to interact with α-mannose, also interacted in an unexpected way with the protective epitope. These cumulative data suggest that structure/activity investigations of the finely tuned C. albicans anti-mannose immune response are worthwhile to increase our basic knowledge and for translation in medicine.
format	article
author	Boualem Sendid Karine Lecointe Mayeul Collot Pierre-Marie Danzé Sébastien Damiens Anne-Sophie Drucbert Chantal Fradin Jean-Pierre Vilcot Frédéric Grenouillet Faustine Dubar Jérôme de Ruyck Samir Jawhara Jean-Maurice Mallet Daniel Poulain
author_facet	Boualem Sendid Karine Lecointe Mayeul Collot Pierre-Marie Danzé Sébastien Damiens Anne-Sophie Drucbert Chantal Fradin Jean-Pierre Vilcot Frédéric Grenouillet Faustine Dubar Jérôme de Ruyck Samir Jawhara Jean-Maurice Mallet Daniel Poulain
author_sort	Boualem Sendid
title	Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes
title_short	Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes
title_full	Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes
title_fullStr	Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes
title_full_unstemmed	Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes
title_sort	dissection of the anti-candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/4979b619fcb54a9b87828257c4e0f296
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Dissection of the anti-Candida albicans mannan immune response using synthetic oligomannosides reveals unique properties of β-1,2 mannotriose protective epitopes

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