CYST WALL ENDOPROTEASES OF ENTAMOEBA INVADENS AND ENTAMOEBA HISTOLYTICA

入侵内阿米巴和溶组织内阿米巴的囊壁内切蛋白酶

• 批准号: 7955937
• 负责人: John C. Samuelson
• 金额: $ 0.47万
• 依托单位: BOSTON UNIVERSITY MEDICAL CAMPUS
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-06-01 至 2010-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955937
• 关键词: Alpha-mannosidase; Amebic colitis; Anabolism; Anti-Retroviral Agents; Biochemical; Biology; Complex; Computer Retrieval of Information on Scientific Projects Database; Concanavalin A; Cyanovirin-N; Cyst; Endoplasmic Reticulum; Entamoeba histolytica; Entamoeba invadens; Funding; Glucosyltransferase; Glucosyltransferases; Glycoproteins; Grant; Institution; Lectin; Link; Liver Abscess; Mass Spectrum Analysis; Medicine; Methods; Polysaccharides; Quality Control; Research; Research Personnel; Resources; Source; Surface; System; United States National Institutes of Health; Upper arm; interest; protein folding; sugar nucleotide

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. N-Glycans of Entamoeba histolytica, the protist that causes amebic dysentery and liver abscess, are of great interest for multiple reasons. E. histolytica makes an unusual truncated N-glycan precursor (Man(5)GlcNAc(2)), has few nucleotide sugar transporters, and has a surface that is capped by the lectin concanavalin A. Here, biochemical and mass spectrometric methods were used to examine N-glycan biosynthesis and the final N-glycans of E. histolytica with the following conclusions. Unprocessed Man(5)GlcNAc(2), which is the most abundant E. histolytica N-glycan, is aggregated into caps on the surface of E. histolytica by the N-glycan-specific, anti-retroviral lectin cyanovirin-N. Glc(1)Man(5)GlcNAc(2), which is made by a UDP-Glc: glycoprotein glucosyltransferase that is part of a conserved N-glycan-dependent endoplasmic reticulum quality control system for protein folding, is also present in mature N-glycans. A swainsonine-sensitive alpha-mannosidase trims some N-glycans to biantennary Man(3)GlcNAc(2). Complex N-glycans of E. histolytica are made by the addition of alpha1,2-linked Gal to both arms of small oligomannose glycans, and Gal residues are capped by one or more Glc. In summary, E. histolytica N-glycans include unprocessed Man(5)GlcNAc(2), which is a target for cyanovirin-N, as well as unique, complex N-glycans containing Gal and Glc.

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