Experientia supplementum (2012)最新文献_第5页

Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis. 基于凝集素和液相色谱的免疫球蛋白(G)糖基化分析方法。

Experientia supplementum (2012) Pub Date : 2021-01-01 DOI: 10.1007/978-3-030-76912-3_2

Tea Petrović, Irena Trbojević-Akmačić

{"title":"Lectin and Liquid Chromatography-Based Methods for Immunoglobulin (G) Glycosylation Analysis.","authors":"Tea Petrović, Irena Trbojević-Akmačić","doi":"10.1007/978-3-030-76912-3_2","DOIUrl":"https://doi.org/10.1007/978-3-030-76912-3_2","url":null,"abstract":"Immunoglobulin (Ig) glycosylation has been shown to dramatically affect its structure and effector functions. Ig glycosylation changes have been associated with different diseases and show a promising biomarker potential for diagnosis and prognosis of disease advancement. On the other hand, therapeutic biomolecules based on structural and functional features of Igs demand stringent quality control during the production process to ensure their safety and efficacy. Liquid chromatography (LC) and lectin-based methods are routinely used in Ig glycosylation analysis complementary to other analytical methods, e.g., mass spectrometry and capillary electrophoresis. This chapter covers analytical approaches based on LC and lectins used in low- and high-throughput N- and O-glycosylation analysis of Igs, with the focus on immunoglobulin G (IgG) applications. General principles and practical examples of the most often used LC methods for Ig purification are described, together with typical workflows for N- and O-glycan analysis on the level of free glycans, glycopeptides, subunits, or intact Igs. Lectin chromatography is a historical approach for the analysis of lectin-carbohydrate interactions and glycoprotein purification but is still being used as a valuable tool in Igs purification and glycan analysis. On the other hand, lectin microarrays have found their application in the rapid screening of glycan profiles on intact proteins.","PeriodicalId":36906,"journal":{"name":"Experientia supplementum (2012)","volume":"112 ","pages":"29-72"},"PeriodicalIF":0.0,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39549101","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Immunoglobulin A Glycosylation and Its Role in Disease. 免疫球蛋白A糖基化及其在疾病中的作用。

Experientia supplementum (2012) Pub Date : 2021-01-01 DOI: 10.1007/978-3-030-76912-3_14

Alyssa L Hansen, Colin Reily, Jan Novak, Matthew B Renfrow

{"title":"Immunoglobulin A Glycosylation and Its Role in Disease.","authors":"Alyssa L Hansen, Colin Reily, Jan Novak, Matthew B Renfrow","doi":"10.1007/978-3-030-76912-3_14","DOIUrl":"https://doi.org/10.1007/978-3-030-76912-3_14","url":null,"abstract":"Human IgA is comprised of two subclasses, IgA1 and IgA2. Monomeric IgA (mIgA), polymeric IgA (pIgA), and secretory IgA (SIgA) are the main molecular forms of IgA. The production of IgA rivals all other immunoglobulin isotypes. The large quantities of IgA reflect the fundamental roles it plays in immune defense, protecting vulnerable mucosal surfaces against invading pathogens. SIgA dominates mucosal surfaces, whereas IgA in circulation is predominately monomeric. All forms of IgA are glycosylated, and the glycans significantly influence its various roles, including antigen binding and the antibody effector functions, mediated by the Fab and Fc portions, respectively. In contrast to its protective role, the aberrant glycosylation of IgA1 has been implicated in the pathogenesis of autoimmune diseases, such as IgA nephropathy (IgAN) and IgA vasculitis with nephritis (IgAVN). Furthermore, detailed characterization of IgA glycosylation, including its diverse range of heterogeneity, is of emerging interest. We provide an overview of the glycosylation observed for each subclass and molecular form of IgA as well as the range of heterogeneity for each site of glycosylation. In many ways, the role of IgA glycosylation is in its early stages of being elucidated. This chapter provides an overview of the current knowledge and research directions.","PeriodicalId":36906,"journal":{"name":"Experientia supplementum (2012)","volume":"112 ","pages":"433-477"},"PeriodicalIF":0.0,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39568551","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 7

Importance and Monitoring of Therapeutic Immunoglobulin G Glycosylation. 治疗性免疫球蛋白G糖基化的重要性及监测。

Experientia supplementum (2012) Pub Date : 2021-01-01 DOI: 10.1007/978-3-030-76912-3_15

Yusuke Mimura, Radka Saldova, Yuka Mimura-Kimura, Pauline M Rudd, Roy Jefferis

{"title":"Importance and Monitoring of Therapeutic Immunoglobulin G Glycosylation.","authors":"Yusuke Mimura, Radka Saldova, Yuka Mimura-Kimura, Pauline M Rudd, Roy Jefferis","doi":"10.1007/978-3-030-76912-3_15","DOIUrl":"https://doi.org/10.1007/978-3-030-76912-3_15","url":null,"abstract":"The complex diantennary-type oligosaccharides at Asn297 residues of the IgG heavy chains have a profound impact on the safety and efficacy of therapeutic IgG monoclonal antibodies (mAbs). Fc glycosylation of a mAb is an established critical quality attribute (CQA), and its oligosaccharide profile is required to be thoroughly characterized by state-of-the-art analytical methods. The Fc oligosaccharides are highly heterogeneous, and the differentially glycosylated species (glycoforms) of IgG express unique biological activities. Glycoengineering is a promising approach for the production of selected mAb glycoforms with improved effector functions, and non- and low-fucosylated mAbs exhibiting enhanced antibody-dependent cellular cytotoxicity activity have been approved or are under clinical evaluation for treatment of cancers, autoimmune/chronic inflammatory diseases, and infection. Recently, the chemoenzymatic glycoengineering method that allows for the transfer of structurally defined oligosaccharides to Asn-linked GlcNAc residues with glycosynthase has been developed for remodeling of IgG-Fc oligosaccharides with high efficiency and flexibility. Additionally, various glycoengineering methods have been developed that utilize the Fc oligosaccharides of IgG as reaction handles to conjugate cytotoxic agents by \"click chemistry\", providing new routes to the design of antibody-drug conjugates (ADCs) with tightly controlled drug-antibody ratios (DARs) and homogeneity. This review focuses on current understanding of the biological relevance of individual IgG glycoforms and advances in the development of next-generation antibody therapeutics with improved efficacy and safety through glycoengineering.","PeriodicalId":36906,"journal":{"name":"Experientia supplementum (2012)","volume":"112 ","pages":"481-517"},"PeriodicalIF":0.0,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39568553","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 4

N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome. n -聚糖生物合成:基本原理及影响结果的因素。

Experientia supplementum (2012) Pub Date : 2021-01-01 DOI: 10.1007/978-3-030-76912-3_7

Teemu Viinikangas, Elham Khosrowabadi, Sakari Kellokumpu

{"title":"N-Glycan Biosynthesis: Basic Principles and Factors Affecting Its Outcome.","authors":"Teemu Viinikangas, Elham Khosrowabadi, Sakari Kellokumpu","doi":"10.1007/978-3-030-76912-3_7","DOIUrl":"https://doi.org/10.1007/978-3-030-76912-3_7","url":null,"abstract":"Carbohydrate chains are the most abundant and diverse of nature's biopolymers and represent one of the four fundamental macromolecular building blocks of life together with proteins, nucleic acids, and lipids. Indicative of their essential roles in cells and in multicellular organisms, genes encoding proteins associated with glycosylation account for approximately 2% of the human genome. It has been estimated that 50-80% of all human proteins carry carbohydrate chains-glycans-as part of their structure. Despite cells utilize only nine different monosaccharides for making their glycans, their order and conformational variation in glycan chains together with chain branching differences and frequent post-synthetic modifications can give rise to an enormous repertoire of different glycan structures of which few thousand is estimated to carry important structural or functional information for a cell. Thus, glycans are immensely versatile encoders of multicellular life. Yet, glycans do not represent a random collection of unpredictable structures but rather, a collection of predetermined but still dynamic entities that are present at defined quantities in each glycosylation site of a given protein in a cell, tissue, or organism.In this chapter, we will give an overview of what is currently known about N-glycan synthesis in higher eukaryotes, focusing not only on the processes themselves but also on factors that will affect or can affect the final outcome-the dynamicity and heterogeneity of the N-glycome. We hope that this review will help understand the molecular details underneath this diversity, and in addition, be helpful for those who plan to produce optimally glycosylated antibody-based therapeutics.","PeriodicalId":36906,"journal":{"name":"Experientia supplementum (2012)","volume":"112 ","pages":"237-257"},"PeriodicalIF":0.0,"publicationDate":"2021-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39549034","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 7

Automation of Immunoglobulin Glycosylation Analysis. 免疫球蛋白糖基化分析自动化。

Experientia supplementum (2012) Pub Date : 2021-01-01 DOI: 10.1007/978-3-030-76912-3_5

Jenifer L Hendel, Richard A Gardner, Daniel I R Spencer

引用次数: 0

Protozoan Parasite Auxotrophies and Metabolic Dependencies. 原生动物寄生虫的营养缺陷和代谢依赖性。

Experientia supplementum (2012) Pub Date : 2018-01-01 DOI: 10.1007/978-3-319-74932-7_9

Elodie Gazanion, Baptiste Vergnes

引用次数: 8

Role of Inflammasomes in the Development of Gastrointestinal Diseases. 炎性小体在胃肠道疾病发展中的作用。

Experientia supplementum (2012) Pub Date : 2018-01-01 DOI: 10.1007/978-3-319-89390-7_10

Mazhar A Kanak, Yoshitaro Shindo, Pavithra SaiKumar, Bashoo Naziruddin

引用次数: 1

Inflammasomes in Clinical Practice: A Brief Introduction. 炎性小体在临床中的应用:简介。

Experientia supplementum (2012) Pub Date : 2018-01-01 DOI: 10.1007/978-3-319-89390-7_1

Elísabet Alcocer-Gómez, Beatriz Castejón-Vega, Macarena López-Sánchez, Mario D Cordero

引用次数: 3

Specific Systems for Evaluation. 具体的评估系统。

Experientia supplementum (2012) Pub Date : 2018-01-01 DOI: 10.1007/978-3-319-78259-1_4

Roderick Adrian Slavcev, Chi Hong Sum, Jesse St Jean, Haein Huh, Nafiseh Nafissi

引用次数: 0

Metabolic Regulation of Innate Immunity to Fungal Infection. 天然免疫对真菌感染的代谢调节。

Experientia supplementum (2012) Pub Date : 2018-01-01 DOI: 10.1007/978-3-319-74932-7_11

Cláudia S Rodrigues, Cláudia F Campos, Cristina Cunha, Agostinho Carvalho

引用次数: 0