Please use this identifier to cite or link to this item: http://scholarbank.nus.edu.sg/handle/10635/32403
Title: N-Glycosylation analysis and comparative modeling of mouse hybridoma lgM84 & 85
Authors: TEO YUNG LING TERENCE
Keywords: IgM, N-glycosylation, human embryonic stem cells, mouse hybridoma, mass spectrometry, comparative modeling
Issue Date: 19-Jan-2012
Source: TEO YUNG LING TERENCE (2012-01-19). N-Glycosylation analysis and comparative modeling of mouse hybridoma lgM84 & 85. ScholarBank@NUS Repository.
Abstract: The application of human embryonic stem cells (hESCs) in regenerative medicine has remained challenging in the last decade, mainly due to potential teratoma formation of undifferentiated hESCs upon administration in vivo. To remove undifferentiated hESCs from the differentiated ones, Bioprocessing Technology Institute (BTI) has generated a mouse hybridoma immunoglobulin M, IgM 84 that exhibits cytotoxic activity via oncosis towards undifferentiated hESCs that are not observed in other IgMs such as IgM 85. Previous findings have shown that IgM 84 and 85 bind to the same surface antigen on undifferentiated hESCs, i.e. podocalyxin-like protein-1. Using comparative modeling, we showed that the 3-dimensional (3D) models for the variable regions of IgM 84 and 85 are not significantly different in structure despite major differences within their complementarity determining regions (CDRs). On the other hand, using techniques such as matrix-assisted laser desorption/ionization mass spectrometry, high pH anionic exchange chromatography etc., we found that IgM 84 to be differently N-glycosylated i.e. improper trimming of high mannose type N-glycans in endoplasmic reticulum (ER), and less fucosylation and sialylation of complex type N-glycans in Golgi, as compared to those on IgM 85. We believe that these differences might suggest a differently folded IgM 84 that could shed more light on how multivalent IgM 84 exhibits its cytotoxicity activity.
URI: http://scholarbank.nus.edu.sg/handle/10635/32403
Appears in Collections:Master's Theses (Open)

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