检索结果-内蒙古大学图书馆

Mass Spectrometric and glycan microarray-Based Characterization of the Filarial Nematode Brugia malayi Glycome Reveals Anionic and Zwitterionic glycan Antigens

引用

MOLECULAR & CELLULAR PROTEOMICS 2022年第5期21卷 100201页

作者： Petralia, Laudine M. C. van Diepen, Angela Lokker, Lena A. Nguyen, D. Linh Sartono, Erliyani Khatri, Vishal Kalyanasundaram, Ramaswamy Taron, Christopher H. Foster, Jeremy M. Hokke, Cornelis H. Leiden Univ Med Ctr Dept Parasitol Ctr Infect Dis Leiden Netherlands New England Biolabs Inc Div Prot Express & Modificat Ipswich MA USA Univ Illinois Dept Biomed Sci Coll Med Rockford Rockford IL USA

Millions of people worldwide are infected with filarial nematodes, responsible for lymphatic filariasis (LF) and other diseases causing chronic disablement. Elimination programs have resulted in a substantial reduction of the rate of infection in certain areas creating a need for improved diagnostic tools to establish robust population surveillance and avoid LF resurgence. glycans from parasitic helminths are emerging as potential antigens for use in diagnostic assays. However, despite its crucial role in host- parasite interactions, filarial glycosylation is still largely, structurally, and functionally uncharacterized. Therefore, we investigated the glycan repertoire of the filarial nematode Brugia malayi. Glycosphingolipid and N-linked glycans were extracted from several life-stages using enzymatic release and characterized using a combination of MALDITOF-MS and glycan sequencing techniques. Next, glycans were purified by HPLC and printed onto microarrays to assess the host anti-glycan antibody response. Comprehensive glycomic analysis of B. malayi revealed the presence of several putative antigenic motifs such as phosphorylcholine and terminal glucuronic acid. glycan microarray screening showed a recognition of most B. malayi glycans by immunoglobulins from rhesus macaques at different time points after infection, which permitted the characterization of the dynamics of anti-glycan immunoglobulin G and M during the establishment of brugian filariasis. A significant level of IgG binding to the parasite glycans was also detected in infected human plasma, while IgG binding to glycans decreased after anthelmintic treatment. Altogether, our work identifies B. malayi glycan antigens and reveals antibody responses from the host that could be exploited as potential markers for LF.

关键词： lymphatic filariasis Brugia malayi N-glycan GSL glycan glycan sequencing glycan microarray antiglycan response antigenic glycans antibodies

来源：评论

学校读者我要写书评

暂无评论

Tools for generating and analyzing glycan microarray data

引用

BEILSTEIN JOURNAL OF ORGANIC CHEMISTRY 2020年 16卷 2260-2271页

作者： Mehta, Akul Y. Heimburg-Molinaro, Jamie Cummings, Richard D. Harvard Med Sch Beth Israel Deaconess Med Ctr Dept Surg Natl Ctr Funct Glyc Boston MA 02215 USA

glycans are one of the major biological polymers found in the mammalian body. They play a vital role in a number of physiologic and pathologic conditions. glycan microarrays allow a plethora of information to be obtained on protein-glycan binding interactions. In this review, we describe the intricacies of the generation of glycan microarray data and the experimental methods for studying binding. We highlight the importance of this knowledge before moving on to the data analysis. We then highlight a number of tools for the analysis of glycan microarray data such as data repositories, data visualization and manual analysis tools, automated analysis tools and structural informatics tools.

关键词： data analysis glycan binding glycan microarray glycomics informatics

来源：评论

学校读者我要写书评

暂无评论

Purification of natural neutral N-glycans by using two-dimensional hydrophilic interaction liquid chromatography x porous graphitized carbon chromatography for glycan-microarray assay

引用

TALANTA 2021年 221卷 121382-121382页

作者： Cao, Cuiyan Yu, Long Yan, Jingyu Fu, Dongmei Yuan, Jingli Liang, Xinmiao Dalian Univ Technol Sch Chem State Key Lab Fine Chem Dalian 116024 Peoples R China Chinese Acad Sci Dalian Inst Chem Phys Key Lab Separat Sci Analyt Chem Dalian 116023 Peoples R China Univ Chinese Acad Sci Beijing 100049 Peoples R China Dalian Polytech Univ Sch Biol Engn Dalian 116034 Peoples R China

glycan microarray for studying carbohydrate-protein interactions requires diverse classes of well-defined glycan standards. In this study, a purification strategy was established based on two-dimensional hydrophilic interaction liquid chromatography and porous graphitized carbon chromatography (HILIC x PGC) for the acquisition of neutral N-glycan standards from natural source. A total of thirty-one N-glycan compounds including seven pairs of isomers with the amounts from 0.7 to 230.0 nmol were isolated from ovalbumin as the model glycoconjugate. The purified N-glycans covered high-mannose, hybrid as well as multi-antenna asymmetric complex types. The purity of majority of these N-glycans was higher than 90%. Detailed structures of the N-glycan compounds were verified via negative ion tandem MS analysis, in which specific diagnostic ions including D- and E -ions were used to identify isomeric and terminal fine structures. The tag-free glycan compounds with well-defined structures, purity and amounts were finally assembled on the glass slide through neoglycolipid technology. Micmarray binding assay of purified glycans with WGA lectin indicated the potential of the established strategy in glycan library expansion and functional glycomics.

关键词： Purification Two-dimensional liquid chromatography Natural N-glycan Negative ion fragmentation glycan microarray

来源：评论

学校读者我要写书评

暂无评论

glycan microarray analysis of the carbohydrate-recognition specificity of native and recombinant forms of the lectin ArtinM

引用

DATA IN BRIEF 2015年 5卷 1035-1047页

作者： Liu, Y. Cecilio, N. T. Carvalho, F. C. Roque-Barreira, M. C. Feizi, T. Imperial Coll London Dept Med Glycosci Lab London England Univ Sao Paulo Fac Med Ribeirao Preto Dept Biol Celular & Mol & Bioagentes Patogen Sao Paulo Brazil

This article contains data related to the researc.h article entitled "Yeast-derived ArtinM shares structure, carbohydrate recognition, and biological effects with native ArtinM" by Cecilio et al. (2015) [1] ArtinM, a D-mannose-binding lectin isolated from the seeds of Artocarpus heterophyllus, exerts immunomodulatory and regenerative activities through its Carbohydrate Recognition Domain (CRD) (Souza et al., 2013;Mariano et al., 2014 [2,3]). The limited availability of the native lectin (n-ArtinM) led us to characterize a recombinant form of the protein, obtained by expression in Saccharomyces cerevisiae (y-ArtinM). We compared the carbohydrate binding specificities of y-ArtinM and n-ArtinM by analyzing the binding of biotinylated preparations of the two lectin forms using a neoglycolipid (NGL)-based glycan microarray. Data showed that y-ArtinM mirrored the specificity exhibited by n-ArtinM. (C) 2015 The Authors. Published by Elsevier Inc.

关键词： glycan microarray Lectin ArtinM Artocarpus heterophyllus Immunomodulation

来源：评论

学校读者我要写书评

暂无评论

Cross-platform comparison of glycan microarray formats

引用

GLYCOBIOLOGY 2014年第6期24卷 507-517页

作者： Wang, Linlin Cummings, Richard D. Smith, David F. Huflejt, Margaret Campbell, Christopher T. Gildersleeve, Jeffrey C. Gerlach, Jared Q. Kilcoyne, Michelle Joshi, Lokesh Serna, Sonia Reichardt, Niels-Christian Pera, Nuria Parera Pieters, Roland J. Eng, William Mahal, Lara K. NYU Dept Chem Biomed Chem Inst New York NY 10003 USA Emory Univ Dept Biochem Glyc Ctr Sch Med Atlanta GA 30322 USA NYU Div Thorac Surg & Thorac Oncol Dept Cardiothorac Surg Sch Med New York NY 10016 USA NCI Chem Biol Lab Ctr Canc Res Frederick Natl Lab Canc Res Frederick MD 21702 USA Natl Univ Ireland Galway Glycosci Grp Natl Ctr Biomed Engn Sci Galway Ireland CICbiomaGUNE Biofunct Nanomat Unit San Sebastian 20009 Spain Univ Utrecht Dept Med Chem & Chem Biol Utrecht Inst Pharmaceut Sci NL-3508 TB Utrecht Netherlands

Carbohydrates participate in almost every aspect of biology from protein sorting to modulating cell differentiation and cell-cell interactions. To date, the majority of data gathered on glycan expression has been obtained via analysis with either anti-glycan antibodies or lectins. A detailed understanding of the specificities of these reagents is critical to the analysis of carbohydrates in biological systems. glycan microarrays are increasingly used to determine the binding specificity of glycan-binding proteins (GBPs). In this study, six different glycan microarray platforms with different modes of glycan presentation were compared using five well-known lectins;concanavalin A, Helix pomatia agglutinin, Maackia amurensis lectin I, Sambucus nigra agglutinin and wheat germ agglutinin. A new method (universal threshold) was developed to facilitate systematic comparisons across distinct array platforms. The strongest binders of each lectin were identified using the universal threshold across all platforms while identification of weaker binders was influenced by platform-specific factors including presentation of determinants, array composition and self-reported thresholding methods. This work compiles a rich dataset for comparative analysis of glycan array platforms and has important implications for the implementation of microarrays in the characterization of GBPs.

关键词： comparison glycan microarray lectin presentation

来源：评论

学校读者我要写书评

暂无评论

Development of a Schistosoma mansoni shotgun O-glycan microarray and application to the discovery of new antigenic schistosome glycan motifs

引用

INTERNATIONAL JOURNAL FOR PARASITOLOGY 2015年第7期45卷 465-475页

作者： van Diepen, Angela van der Plas, Arend-Jan Kozak, Radoslaw P. Royle, Louise Dunne, David W. Hokke, Cornelis H. Leiden Univ Dept Parasitol Ctr Infect Dis Med Ctr NL-2300 RC Leiden Netherlands Ludger Ltd Culham Sci Ctr Abingdon OX14 3EB Oxon England Univ Cambridge Dept Pathol Cambridge CB2 1TN England

Upon infection with Schistosoma, antibody responses are mounted that are largely directed against glycans. Over the last few years significant progress has been made in characterising the antigenic properties of N-glycans of Schistosoma mansoni. Despite also being abundantly expressed by schistosomes, much less is understood about O-glycans and antibody responses to these have not yet been systematically analysed. Antibody binding to schistosome glycans can be analysed efficiently and quantitatively using glycan microarrays, but O-glycan array construction and exploration is lagging behind because no universal O-glycanase is available, and release of O-glycans has been dependent on chemical methods. Recently, a modified hydrazinolysis method has been developed that allows the release of O-glycans with free reducing termini and limited degradation, and we applied this method to obtain O-glycans from different S. mansoni life stages. Two-dimensional HPLC separation of 2-aminobenzoic acid-labelled O-glycans generated 362 O-glycan-containing fractions that were printed on an epoxide-modified glass slide, thereby generating the first shotgun O-glycan microarray containing naturally occurring schistosome O-glycans. Monoclonal antibodies and mass spectrometry showed that the O-glycan microarray contains well-known antigenic glycan motifs as well as numerous other, potentially novel, antibody targets. Incubations of the microarrays with sera from Schistosoma-infected humans showed substantial antibody responses to O-glycans in addition to those observed to the previously investigated N- and glycosphingolipid glycans. This underlines the importance of the inclusion of these often schistosome-specific O-glycans in glycan antigen studies and indicates that O-glycans contain novel antigenic motifs that have potential for use in diagnostic methods and studies aiming at the discovery of vaccine targets. (C) 2015 The Authors. Published by Elsevier Ltd. on behalf of Australian Soci

关键词： Antibodies glycan microarray O-glycans Schistosoma

来源：评论

学校读者我要写书评

暂无评论

Antigenicity evaluation of the synthetic trisaccharides related to Plesiomonas shigelloides serotype O51 O-antigen containing an acetamidino group

引用

CARBOHYDRATE RESEARCH 2025年 550卷 109388页

作者： Qin, Chunjun Han, Wei Tian, Guangzong Zou, Xiaopeng Maciejewska, Anna Lukasiewicz, Jolanta Seeberger, Peter H. Hu, Jing Yin, Jian Jiangnan Univ Sch Biotechnol Lihu Ave 1800 Wuxi 214122 Peoples R China Jiangnan Univ Key Lab Carbohydrate Chem & Biotechnol Minist Educ Lihu Ave 1800 Wuxi 214122 Peoples R China Jiangnan Univ Wuxi Sch Med Lihu Ave 1800 Wuxi 214122 Peoples R China Max Planck Inst Colloids & Interfaces Biomol Syst Dept Am Muhlenberg 1 D-14476 Potsdam Germany Polish Acad Sci Ludw Hirszfeld Inst Immunol & Expt Therapy Lab Microbial Immunochemistry & Vaccines PL-53114 Wroclaw Poland Jiangnan Univ Sch Life Sci & Hlth Engn Lihu Ave 1800 Wuxi 214122 Peoples R China Jiangnan Univ Innovat Ctr Vaccine Engn Lihu Ave 1800 Wuxi 214122 Peoples R China

Bacterial surface polysaccharides are widely decorated with diverse rare functional groups. An understanding of the role of these functional groups in immunological activity of the glycans is required for the development of carbohydrate-based treatment against bacterial infectious diseases. Here, the antigenicity evaluation of synthetic trisaccharide 1 related to Plesiomonas shigelloides serotype O51 lipopolysaccharide (LPS) O-antigen and its acetamido derivative 2 was achieved to elucidate the immunological importance of O-antigen structure. The rabbit antisera with high titers of IgG and IgM were collected after immunization with purified P. shigelloides serotype O51 LPS. glycan microarray screening results showed that both IgG and IgM in rabbit antisera bound specifically to trisaccharides 1 and 2, indicating that the trisaccharide repeating unit is a key antigenic epitope of P. shigelloides serotype O51 O-antigen, while the acetamidino group has no influence on the antigenicity. This finding provides key information for glycoconjugate vaccine design for P. shigelloides serotype O51.

关键词： Plesiomonas shigelloides O -Antigen Acetamidino group Synthetic oligosaccharide glycan microarray Antigenicity

来源：评论

学校读者我要写书评

暂无评论

Comprehensive Modular Synthesis of Ganglioside glycans and Evaluation of their Binding Affinities to Siglec-7 and Siglec-9

引用

ADVANCED SCIENCE 2025年第2期12卷 e2412815页

作者： Adak, Avijit K. Tseng, Hsin-Kai Chang, Shu-Yen Chiang, Yu-Ching Lyu, Ke-Hong Lee, Yun-Sheng Lu, Wen Kuo, Wen-Hua Angata, Takashi Lin, Chun-Cheng Natl Tsing Hua Univ Dept Chem 101 Sect 2Kuang Fu Rd Hsinchu 30013 Taiwan Acad Sinica Inst Biol Chem Taipei 11529 Taiwan Kaohsiung Med Univ Dept Med & Appl Chem Kaohsiung 80708 Taiwan

In the present work, bacterial glycosyltransferases are utilized to construct ganglioside glycans in a convergent approach via a *** regeneration system and one-pot multienzyme reactions. Starting from beta-lactoside enables the diversification of both the glycan moieties and the linkages in the lower alpha-arm and upper beta-arm. Overall, a comprehensive panel of 24 natural a-series (GM3, GM2, GM1a, GD1a, GT1a, and fucosyl-GM1), b-series (GD3, GD2, GD1b, GT1b, and GQ1b), c-series (GT3, GT2, GT1c, GQ1c, and GP1c), alpha-series (GM1 alpha, GD1a alpha, and GT1a alpha), and o-series (GA2, GA1, GM1b, GalNAc-GM1b, and GD1c) ganglioside glycans are prepared, which are suitable for biological studies and further applications. Moreover, a microarray is constructed with these synthesized ganglioside glycans to investigate their binding specificity with recombinant Fc-fused Siglec-7 and Siglec-9, which are immune checkpoint-like glycan recognition proteins on natural killer cells. The microarray binding results reveal that GD3 and GT1a alpha are specific ligands for Siglec-7 and Siglec-9, respectively, and this discovery can lead to the identification of appropriate ligands for investigating the roles of these Siglecs in immunomodulation.

关键词： carbohydrates chemoenzymatic synthesis gangliosides glycan microarray Siglec

来源：评论

学校读者我要写书评

暂无评论

Insights into biofilm architecture and maturation enable improved clinical strategies for exopolysaccharide-targeting therapeutics

引用

CELL CHEMICAL BIOLOGY 2024年第12期31卷 2096-2111.e7页

作者： Temme, J. Sebastian Tan, Zibin Li, Mi Yang, Mo Wlodawer, Alexander Huang, Xuefei Schneekloth, John S. Gildersleeve, Jeffrey C. NCI Ctr Canc Res Chem Biol Lab Frederick MD 21702 USA Michigan State Univ Dept Chem 578 S Shaw Lane E Lansing MI 48824 USA Michigan State Univ Inst Quantitat Hlth Sci & Engn E Lansing MI 48824 USA NCI Ctr Struct Biol Ctr Canc Res Frederick MD 21702 USA Frederick Natl Lab Canc Res Basic Sci Program Frederick MD 21702 USA Michigan State Univ Dept Biomed Engn E Lansing MI 48824 USA

Polysaccharide intercellular adhesin (PIA), an exopolysaccharide composed of poly-N-acetyl glucosamine (PNAG), is an essential component in many pathogenic biofilms. Partial deacetylation of PNAG is required for biofilm formation, but limited structural knowledge hinders therapeutic development. Employing a new monoclonal antibody (TG10) that selectively binds highly deacetylated PNAG and an antibody (F598) in clinical trials that binds highly acetylated PNAG, we demonstrate that PIA within the biofilm contains distinct regions of highly acetylated and deacetylated exopolysaccharide, contrary to the previous model invoking stochastic deacetylation throughout the biofilm. This discovery led us to hypothesize that targeting both forms of PNAG would enhance efficacy. Remarkably, TG10 and F598 synergistically increased in vitro and in vivo activity, providing 90% survival in a lethal Staphylococcus aureus challenge murine model. Our advanced model deepens the conceptual understanding of PIA architecture and maturation and reveals improved design strategies for PIA-targeting therapeutics, vaccines, and diagnostic agents.

关键词： PIA PNAG anti-glycan antibodies glycan microarray SPRi array confocal microscopy biofilm Staphylococcal infections TG10 F598

来源：评论

学校读者我要写书评

暂无评论

Simple and practical sialoglycan encoding system reveals vast diversity in nature and identifies a universal sialoglycan-recognizing probe derived from AB5 toxin B subunits

引用

GLYCOBIOLOGY 2022年第12期32卷 1101-1115页

作者： Sasmal, Aniruddha Khan, Naazneen Khedri, Zahra Kellman, Benjamin P. Srivastava, Saurabh Verhagen, Andrea Yu, Hai Bruntse, Anders Bech Diaz, Sandra Varki, Nissi Beddoe, Travis Paton, Adrienne W. Paton, James C. Chen, Xi Lewis, Nathan E. Varki, Ajit Univ Calif San Diego Glycobiol Res & Training Ctr La Jolla CA 92093 USA Univ Calif San Diego Dept Cellular & Mol Med La Jolla CA 92093 USA Univ Calif San Diego Dept Pediat La Jolla CA 92093 USA Univ Calif Davis Dept Chem Davis CA 95616 USA La Trobe Univ Dept Anim Plant & Soil Sci Bundoora Vic 3086 Australia La Trobe Univ Ctr AgriBiosci Bundoora Vic 3086 Australia Univ Adelaide Res Ctr Infect Dis Dept Mol & Biomed Sci Adelaide SA 5005 Australia Univ Calif San Diego Dept Med La Jolla CA 92093 USA

Vertebrate sialic acids (Sias) display much diversity in modifications, linkages, and underlying glycans. Slide microarrays allow high-throughput explorations of sialoglycan-protein interactions. A microarray presenting similar to 150 structurally defined sialyltrisaccharides with various Sias linkages and modifications still poses challenges in planning, data sorting, visualization, and analysis. To address these issues, we devised a simple 9-digit code for sialyltrisaccharides with terminal Sias and underlying two monosaccharides assigned from the nonreducing end, with 3 digits assigning a monosaccharide, its modifications, and linkage. Calculations based on the encoding system reveal >113,000 likely linear sialyltrisaccharides in nature. Notably, a biantennary N-glycan with 2 terminal sialyltrisaccharides could thus have >10(10) potential combinations and a triantennary N-glycan with 3 terminal sequences, >10(15) potential combinations. While all possibilities likely do not exist in nature, sialoglycans encode enormous diversity. While glycomic approaches are used to probe such diverse sialomes, naturally occurring bacterial AB(5) toxin B subunits are simpler tools to track the dynamic sialome in biological systems. Sialoglycan microarray was utilized to compare sialoglycan-recognizing bacterial toxin B subunits. Unlike the poor correlation between B subunits and species phylogeny, there is stronger correlation with Sia-epitope preferences. Further supporting this pattern, we report a B subunit (YenB) from Yersinia enterocolitica (broad host range) recognizing almost all sialoglycans in the microarray, including 4-O-acetylated-Sias not recognized by a Yersinia pestis orthologue (YpeB). Differential Sia-binding patterns were also observed with phylogenetically related B subunits from Escherichia coli (SubB), Salmonella Typhi (PltB), Salmonella Typhimurium (ArtB), extra-intestinal *** (EcPltB), Vibrio cholera (CtxB), and cholera family homologue of E. coli (EcxB

关键词： glycan microarray glycan coding bacterial toxin toxin B subunit Yersinia enterocolitica

来源：评论

学校读者我要写书评

暂无评论

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

请选择保存的检索档案：

请选择收藏分类：

通借通还

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：