The glycointeractome of serogroup B Neisseria meningitidis strain MC58

Abstract Neisseria meningitidis express numerous virulence factors that enable it to interact with diverse microenvironments within the host, during both asymptomatic nasopharyngeal colonization and invasive disease. Many of these interactions involve bacterial or host glycans. In order to character...

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Autores principales:	Tsitsi D. Mubaiwa, Lauren E. Hartley-Tassell, Evgeny A. Semchenko, Freda. E.-C. Jen, Yogitha N. Srikhanta, Christopher J. Day, Michael P. Jennings, Kate L. Seib
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/8379f6aa7cdc420585fd4f2d973b774a
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spelling	oai:doaj.org-article:8379f6aa7cdc420585fd4f2d973b774a2021-12-02T16:07:00ZThe glycointeractome of serogroup B Neisseria meningitidis strain MC5810.1038/s41598-017-05894-w2045-2322https://doaj.org/article/8379f6aa7cdc420585fd4f2d973b774a2017-07-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-05894-whttps://doaj.org/toc/2045-2322Abstract Neisseria meningitidis express numerous virulence factors that enable it to interact with diverse microenvironments within the host, during both asymptomatic nasopharyngeal colonization and invasive disease. Many of these interactions involve bacterial or host glycans. In order to characterise the meningococcal glycointeractome, glycan arrays representative of structures found on human cells, were used as a screening tool to investigate host glycans bound by N. meningitidis. Arrays probed with fluorescently labelled wild-type MC58 revealed binding to 223 glycans, including blood group antigens, mucins, gangliosides and glycosaminoglycans. Mutant strains lacking surface components, including capsule, lipooligosaccharide (LOS), Opc and pili, were investigated to identify the factors responsible for glycan binding. Surface plasmon resonance and isothermal calorimetry were used to confirm binding and determine affinities between surface components and host glycans. We observed that the L3 LOS immunotype (whole cells and purified LOS) bound 26 structures, while L8 only bound 5 structures. We further demonstrated a direct glycan-glycan interaction between purified L3 LOS and Thomsen–Friedenreich (TF) antigen, with a KD of 13 nM. This is the highest affinity glycan-glycan interaction reported to date. These findings highlight the diverse glycointeractions that may occur during different stages of meningococcal disease, which could be exploited for development of novel preventative and therapeutic strategies.Tsitsi D. MubaiwaLauren E. Hartley-TassellEvgeny A. SemchenkoFreda. E.-C. JenYogitha N. SrikhantaChristopher J. DayMichael P. JenningsKate L. SeibNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tsitsi D. Mubaiwa Lauren E. Hartley-Tassell Evgeny A. Semchenko Freda. E.-C. Jen Yogitha N. Srikhanta Christopher J. Day Michael P. Jennings Kate L. Seib The glycointeractome of serogroup B Neisseria meningitidis strain MC58
description	Abstract Neisseria meningitidis express numerous virulence factors that enable it to interact with diverse microenvironments within the host, during both asymptomatic nasopharyngeal colonization and invasive disease. Many of these interactions involve bacterial or host glycans. In order to characterise the meningococcal glycointeractome, glycan arrays representative of structures found on human cells, were used as a screening tool to investigate host glycans bound by N. meningitidis. Arrays probed with fluorescently labelled wild-type MC58 revealed binding to 223 glycans, including blood group antigens, mucins, gangliosides and glycosaminoglycans. Mutant strains lacking surface components, including capsule, lipooligosaccharide (LOS), Opc and pili, were investigated to identify the factors responsible for glycan binding. Surface plasmon resonance and isothermal calorimetry were used to confirm binding and determine affinities between surface components and host glycans. We observed that the L3 LOS immunotype (whole cells and purified LOS) bound 26 structures, while L8 only bound 5 structures. We further demonstrated a direct glycan-glycan interaction between purified L3 LOS and Thomsen–Friedenreich (TF) antigen, with a KD of 13 nM. This is the highest affinity glycan-glycan interaction reported to date. These findings highlight the diverse glycointeractions that may occur during different stages of meningococcal disease, which could be exploited for development of novel preventative and therapeutic strategies.
format	article
author	Tsitsi D. Mubaiwa Lauren E. Hartley-Tassell Evgeny A. Semchenko Freda. E.-C. Jen Yogitha N. Srikhanta Christopher J. Day Michael P. Jennings Kate L. Seib
author_facet	Tsitsi D. Mubaiwa Lauren E. Hartley-Tassell Evgeny A. Semchenko Freda. E.-C. Jen Yogitha N. Srikhanta Christopher J. Day Michael P. Jennings Kate L. Seib
author_sort	Tsitsi D. Mubaiwa
title	The glycointeractome of serogroup B Neisseria meningitidis strain MC58
title_short	The glycointeractome of serogroup B Neisseria meningitidis strain MC58
title_full	The glycointeractome of serogroup B Neisseria meningitidis strain MC58
title_fullStr	The glycointeractome of serogroup B Neisseria meningitidis strain MC58
title_full_unstemmed	The glycointeractome of serogroup B Neisseria meningitidis strain MC58
title_sort	glycointeractome of serogroup b neisseria meningitidis strain mc58
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/8379f6aa7cdc420585fd4f2d973b774a
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The glycointeractome of serogroup B Neisseria meningitidis strain MC58

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