Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry

Autores
Palma, Angelina S.; Liu, Yan; Zhang, Hongtao; Zhang, Yibing; McCleary, Barry V.; Yu, Guangli; Huang, Qilin; Guidolin, Leticia Soledad; Ciocchini, Andres Eduardo; Torosantucci, Antonella; Wang, Denong; Carvalho, Ana Luísa; Fontes, Carlos M. G. A.; Mulloy, Barbara; Childs, Robert A.; Feizi, Ten; Chai, Wengang
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glucans are polymers of D-glucose with differing linkages in linear or branched sequences. They are constituents of microbial and plant cell-walls and involved in important bio-recognition processes, including immunomodulation, anticancer activities, pathogen virulence, and plant cellwall biodegradation. Translational possibilities for these activities in medicine and biotechnology are considerable. High-throughput micro-methods are needed to screen proteins for recognition of specific glucan sequences as a lead to structure-function studies and their exploitation. We describe construction of a "glucome" microarray, the first sequence-defined glycome-scale microarray, using a "designer" approach from targeted ligand-bearing glucans in conjunction with a novel high-sensitivity mass spectrometric sequencing method, as a screening tool to assign glucan recognition motifs. The glucome microarray comprises 153 oligosaccharide probes with high purity, representing major sequences in glucans. Negative-ion electrospray tandem mass spectrometry with collision-induced dissociation was used for complete linkage analysis of gluco-oligosaccharides in linear "homo" and "hetero" and branched sequences. The system is validated using antibodies and carbohydrate-binding modules known to target α- or β-glucans in different biological contexts, extending knowledge on their specificities, and applied to reveal new information on glucan recognition by two signaling molecules of the immune system against pathogens: Dectin-1 and DC-SIGN. The sequencing of the glucan oligosaccharides by the MS method and their interrogation on the microarrays provides detailed information on linkage, sequence and chain length requirements of glucan-recognizing proteins, and are a sensitive means of revealing unsuspected sequences in the polysaccharides.
Fil: Palma, Angelina S.. Imperial College London; Reino Unido. Universidade de Lisboa; Portugal
Fil: Liu, Yan. Imperial College London; Reino Unido
Fil: Zhang, Hongtao. Imperial College London; Reino Unido. Jiangnan University; China
Fil: Zhang, Yibing. Imperial College London; Reino Unido
Fil: McCleary, Barry V.. Megazyme International Ireland; Irlanda
Fil: Yu, Guangli. Ocean University Of China; China
Fil: Huang, Qilin. Huazhong Agricultural University; China. Wuhan University; China
Fil: Guidolin, Leticia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Ciocchini, Andres Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Torosantucci, Antonella. Istituto Superiore Di Sanita; Italia
Fil: Wang, Denong. Sri International; Estados Unidos
Fil: Carvalho, Ana Luísa. Universidade de Lisboa; Portugal
Fil: Fontes, Carlos M. G. A.. Universidade de Lisboa; Portugal
Fil: Mulloy, Barbara. Imperial College London; Reino Unido
Fil: Childs, Robert A.. Imperial College London; Reino Unido
Fil: Feizi, Ten. Imperial College London; Reino Unido
Fil: Chai, Wengang. Imperial College London; Reino Unido
Materia
Glucan
Glucan Recognition Motifs
Oligosaccharides
Microarray
Mass Spectrometry
Glycome
Glucome
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/38692
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/38692
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometryPalma, Angelina S.Liu, YanZhang, HongtaoZhang, YibingMcCleary, Barry V.Yu, GuangliHuang, QilinGuidolin, Leticia SoledadCiocchini, Andres EduardoTorosantucci, AntonellaWang, DenongCarvalho, Ana LuísaFontes, Carlos M. G. A.Mulloy, BarbaraChilds, Robert A.Feizi, TenChai, WengangGlucanGlucan Recognition MotifsOligosaccharidesMicroarrayMass SpectrometryGlycomeGlucomehttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Glucans are polymers of D-glucose with differing linkages in linear or branched sequences. They are constituents of microbial and plant cell-walls and involved in important bio-recognition processes, including immunomodulation, anticancer activities, pathogen virulence, and plant cellwall biodegradation. Translational possibilities for these activities in medicine and biotechnology are considerable. High-throughput micro-methods are needed to screen proteins for recognition of specific glucan sequences as a lead to structure-function studies and their exploitation. We describe construction of a "glucome" microarray, the first sequence-defined glycome-scale microarray, using a "designer" approach from targeted ligand-bearing glucans in conjunction with a novel high-sensitivity mass spectrometric sequencing method, as a screening tool to assign glucan recognition motifs. The glucome microarray comprises 153 oligosaccharide probes with high purity, representing major sequences in glucans. Negative-ion electrospray tandem mass spectrometry with collision-induced dissociation was used for complete linkage analysis of gluco-oligosaccharides in linear "homo" and "hetero" and branched sequences. The system is validated using antibodies and carbohydrate-binding modules known to target α- or β-glucans in different biological contexts, extending knowledge on their specificities, and applied to reveal new information on glucan recognition by two signaling molecules of the immune system against pathogens: Dectin-1 and DC-SIGN. The sequencing of the glucan oligosaccharides by the MS method and their interrogation on the microarrays provides detailed information on linkage, sequence and chain length requirements of glucan-recognizing proteins, and are a sensitive means of revealing unsuspected sequences in the polysaccharides.Fil: Palma, Angelina S.. Imperial College London; Reino Unido. Universidade de Lisboa; PortugalFil: Liu, Yan. Imperial College London; Reino UnidoFil: Zhang, Hongtao. Imperial College London; Reino Unido. Jiangnan University; ChinaFil: Zhang, Yibing. Imperial College London; Reino UnidoFil: McCleary, Barry V.. Megazyme International Ireland; IrlandaFil: Yu, Guangli. Ocean University Of China; ChinaFil: Huang, Qilin. Huazhong Agricultural University; China. Wuhan University; ChinaFil: Guidolin, Leticia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Ciocchini, Andres Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); ArgentinaFil: Torosantucci, Antonella. Istituto Superiore Di Sanita; ItaliaFil: Wang, Denong. Sri International; Estados UnidosFil: Carvalho, Ana Luísa. Universidade de Lisboa; PortugalFil: Fontes, Carlos M. G. A.. Universidade de Lisboa; PortugalFil: Mulloy, Barbara. Imperial College London; Reino UnidoFil: Childs, Robert A.. Imperial College London; Reino UnidoFil: Feizi, Ten. Imperial College London; Reino UnidoFil: Chai, Wengang. Imperial College London; Reino UnidoAmerican Society for Biochemistry and Molecular Biology2015-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/38692Palma, Angelina S.; Liu, Yan; Zhang, Hongtao; Zhang, Yibing; McCleary, Barry V.; et al.; Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry; American Society for Biochemistry and Molecular Biology; Molecular & Cellular Proteomics; 14; 4; 4-2015; 974-9881535-9476CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1074/mcp.M115.048272info:eu-repo/semantics/altIdentifier/url/http://www.mcponline.org/content/14/4/974.longinfo:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390274/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:46:48Zoai:ri.conicet.gov.ar:11336/38692instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 09:46:49.03CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
title Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
spellingShingle Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
Palma, Angelina S.
Glucan
Glucan Recognition Motifs
Oligosaccharides
Microarray
Mass Spectrometry
Glycome
Glucome
title_short Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
title_full Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
title_fullStr Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
title_full_unstemmed Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
title_sort Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry
dc.creator.none.fl_str_mv Palma, Angelina S.
Liu, Yan
Zhang, Hongtao
Zhang, Yibing
McCleary, Barry V.
Yu, Guangli
Huang, Qilin
Guidolin, Leticia Soledad
Ciocchini, Andres Eduardo
Torosantucci, Antonella
Wang, Denong
Carvalho, Ana Luísa
Fontes, Carlos M. G. A.
Mulloy, Barbara
Childs, Robert A.
Feizi, Ten
Chai, Wengang
author Palma, Angelina S.
author_facet Palma, Angelina S.
Liu, Yan
Zhang, Hongtao
Zhang, Yibing
McCleary, Barry V.
Yu, Guangli
Huang, Qilin
Guidolin, Leticia Soledad
Ciocchini, Andres Eduardo
Torosantucci, Antonella
Wang, Denong
Carvalho, Ana Luísa
Fontes, Carlos M. G. A.
Mulloy, Barbara
Childs, Robert A.
Feizi, Ten
Chai, Wengang
author_role author
author2 Liu, Yan
Zhang, Hongtao
Zhang, Yibing
McCleary, Barry V.
Yu, Guangli
Huang, Qilin
Guidolin, Leticia Soledad
Ciocchini, Andres Eduardo
Torosantucci, Antonella
Wang, Denong
Carvalho, Ana Luísa
Fontes, Carlos M. G. A.
Mulloy, Barbara
Childs, Robert A.
Feizi, Ten
Chai, Wengang
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Glucan
Glucan Recognition Motifs
Oligosaccharides
Microarray
Mass Spectrometry
Glycome
Glucome
topic Glucan
Glucan Recognition Motifs
Oligosaccharides
Microarray
Mass Spectrometry
Glycome
Glucome
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Glucans are polymers of D-glucose with differing linkages in linear or branched sequences. They are constituents of microbial and plant cell-walls and involved in important bio-recognition processes, including immunomodulation, anticancer activities, pathogen virulence, and plant cellwall biodegradation. Translational possibilities for these activities in medicine and biotechnology are considerable. High-throughput micro-methods are needed to screen proteins for recognition of specific glucan sequences as a lead to structure-function studies and their exploitation. We describe construction of a "glucome" microarray, the first sequence-defined glycome-scale microarray, using a "designer" approach from targeted ligand-bearing glucans in conjunction with a novel high-sensitivity mass spectrometric sequencing method, as a screening tool to assign glucan recognition motifs. The glucome microarray comprises 153 oligosaccharide probes with high purity, representing major sequences in glucans. Negative-ion electrospray tandem mass spectrometry with collision-induced dissociation was used for complete linkage analysis of gluco-oligosaccharides in linear "homo" and "hetero" and branched sequences. The system is validated using antibodies and carbohydrate-binding modules known to target α- or β-glucans in different biological contexts, extending knowledge on their specificities, and applied to reveal new information on glucan recognition by two signaling molecules of the immune system against pathogens: Dectin-1 and DC-SIGN. The sequencing of the glucan oligosaccharides by the MS method and their interrogation on the microarrays provides detailed information on linkage, sequence and chain length requirements of glucan-recognizing proteins, and are a sensitive means of revealing unsuspected sequences in the polysaccharides.
Fil: Palma, Angelina S.. Imperial College London; Reino Unido. Universidade de Lisboa; Portugal
Fil: Liu, Yan. Imperial College London; Reino Unido
Fil: Zhang, Hongtao. Imperial College London; Reino Unido. Jiangnan University; China
Fil: Zhang, Yibing. Imperial College London; Reino Unido
Fil: McCleary, Barry V.. Megazyme International Ireland; Irlanda
Fil: Yu, Guangli. Ocean University Of China; China
Fil: Huang, Qilin. Huazhong Agricultural University; China. Wuhan University; China
Fil: Guidolin, Leticia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Ciocchini, Andres Eduardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús). Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas "Dr. Raúl Alfonsín" (sede Chascomús); Argentina
Fil: Torosantucci, Antonella. Istituto Superiore Di Sanita; Italia
Fil: Wang, Denong. Sri International; Estados Unidos
Fil: Carvalho, Ana Luísa. Universidade de Lisboa; Portugal
Fil: Fontes, Carlos M. G. A.. Universidade de Lisboa; Portugal
Fil: Mulloy, Barbara. Imperial College London; Reino Unido
Fil: Childs, Robert A.. Imperial College London; Reino Unido
Fil: Feizi, Ten. Imperial College London; Reino Unido
Fil: Chai, Wengang. Imperial College London; Reino Unido
description Glucans are polymers of D-glucose with differing linkages in linear or branched sequences. They are constituents of microbial and plant cell-walls and involved in important bio-recognition processes, including immunomodulation, anticancer activities, pathogen virulence, and plant cellwall biodegradation. Translational possibilities for these activities in medicine and biotechnology are considerable. High-throughput micro-methods are needed to screen proteins for recognition of specific glucan sequences as a lead to structure-function studies and their exploitation. We describe construction of a "glucome" microarray, the first sequence-defined glycome-scale microarray, using a "designer" approach from targeted ligand-bearing glucans in conjunction with a novel high-sensitivity mass spectrometric sequencing method, as a screening tool to assign glucan recognition motifs. The glucome microarray comprises 153 oligosaccharide probes with high purity, representing major sequences in glucans. Negative-ion electrospray tandem mass spectrometry with collision-induced dissociation was used for complete linkage analysis of gluco-oligosaccharides in linear "homo" and "hetero" and branched sequences. The system is validated using antibodies and carbohydrate-binding modules known to target α- or β-glucans in different biological contexts, extending knowledge on their specificities, and applied to reveal new information on glucan recognition by two signaling molecules of the immune system against pathogens: Dectin-1 and DC-SIGN. The sequencing of the glucan oligosaccharides by the MS method and their interrogation on the microarrays provides detailed information on linkage, sequence and chain length requirements of glucan-recognizing proteins, and are a sensitive means of revealing unsuspected sequences in the polysaccharides.
publishDate 2015
dc.date.none.fl_str_mv 2015-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/38692
Palma, Angelina S.; Liu, Yan; Zhang, Hongtao; Zhang, Yibing; McCleary, Barry V.; et al.; Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry; American Society for Biochemistry and Molecular Biology; Molecular & Cellular Proteomics; 14; 4; 4-2015; 974-988
1535-9476
CONICET Digital
CONICET
url http://hdl.handle.net/11336/38692
identifier_str_mv Palma, Angelina S.; Liu, Yan; Zhang, Hongtao; Zhang, Yibing; McCleary, Barry V.; et al.; Unravelling glucan recognition systems by glycome microarrays using the designer approach and mass spectrometry; American Society for Biochemistry and Molecular Biology; Molecular & Cellular Proteomics; 14; 4; 4-2015; 974-988
1535-9476
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/url/http://www.mcponline.org/content/14/4/974.long
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4390274/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
publisher.none.fl_str_mv American Society for Biochemistry and Molecular Biology
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
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reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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