Cytochemical study of tegument surface membrane in Schistosoma japonicum and Schistosoma mekongi using lectin stains
Issued Date
2024
Copyright Date
1989
Resource Type
Language
eng
File Type
application/pdf
No. of Pages/File Size
xxi, 229 leaves : ill.
Access Rights
open access
Rights
ผลงานนี้เป็นลิขสิทธิ์ของมหาวิทยาลัยมหิดล ขอสงวนไว้สำหรับเพื่อการศึกษาเท่านั้น ต้องอ้างอิงแหล่งที่มา ห้ามดัดแปลงเนื้อหา และห้ามนำไปใช้เพื่อการค้า
Rights Holder(s)
Mahidol University
Bibliographic Citation
Thesis (M.Sc. (Anatomy))--Mahidol University, 1989
Suggested Citation
Wilaiwan Mothong Cytochemical study of tegument surface membrane in Schistosoma japonicum and Schistosoma mekongi using lectin stains. Thesis (M.Sc. (Anatomy))--Mahidol University, 1989. Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/99094
Title
Cytochemical study of tegument surface membrane in Schistosoma japonicum and Schistosoma mekongi using lectin stains
Alternative Title(s)
การศึกษาทางไซโคเคมีของผิวพยาธิใบไม้ในเลือด Schistosoma japonicum และ Schistosoma mekongi
Author(s)
Advisor(s)
Abstract
The carbohydrate moieties of glycoproteins and / or glycolipids have been proven to be the major epitopes of antigens on the schistosome tegument. In the present study, by using lectins as probes, both the carbohydrate moieties on the surface membrane and in the tegument glycoproteins were examined by LM, TEM and electroblotting techniques. By using Avidin-Biotin-Lectin labelling, it was revealed that there were binding sites for concanavalin A (Con A), wheat germ agglutinin (WGA), Ricinus communis I (RCA I), peanut agglutinin (PNA), soybean aggtutinin (SBA) and Ulex europaeus I (UEA I) on the surface membrane of adult Oriental schistosomes. At both LM and TEM levels, the binding patterns of these lectins were generally similar; that is, the binding was strong on the dorsal and lateral aspects of the parasites surface membrane, while the membrane of the gynecophoral canal showed only light binding. However, there was slight but significant difference in the distribution and stainging intensity between Con A and WGA in one group versus RCA I, PNA, SBA and UEA I in another group. Con A and WGA intensely stained the membrane covering the upper part of pits and UEA I stained only on the upper half of ridges membrane. This, therefore, implied the presence of D-mannose/D-glucose, N-acetyl-D-glucosamine/sialic acid, D-galactose, N-acetyl-D-galactosamine, and L-fucose residues on the membrane of adult Oriental schistosomes, with the four former residues (detected by Con A and WGA) localized extensively on the pits and ridges membrane, while the latter three (detected by RCA I, PNA, SBA and UEA I) resided preferentially on the membrane covering the upper half of ridges. The binding of these lectins to the tegument glycoproteins separated in SDS-PAGE and electroblotted onto NC sheets indicated that there appeared to have similar compositions but probably different quantities of D-mannose/D-glucose, N-acetyl-D-glucosamine/sialic acid, N-acetyl-D-galactosamine, L-fucose residues (detected by Con A, WGA, SBA, UEA I, respectively) in all three species of adult schistosomes, and totally there were 42, 36, 29 bands of tegument proteins in S. japonicum, S. mekongi, S. mansoni ranging in MW from >205,000 to 14,000. The tegument glycoproteins that contained D-galactose and D-galactose-N-acetyl-D-galactosamine residues (detected by RCA I and PNA) probably have larger amount in adult S. japonicum (Chinese, Philippine) than in S. mekongi and S. mansoni. The immunoblot patterns as revealed by the treatments with mouse antisera against S. japonicum (Chinese-ISCH : Philippine-ISPH), S. mekongi (ISME) and S. mansoni (ISMA) indicated that there were at least 8 common antigens in both strains of S. japonicum (Chinese, Philippine) at MW of 110,000, 98,000, 68,000, 47,000, 45,000 28,000, 27,000, 26,000, and that the latter three bands might be specific antigens for this species. In S. mekongi, there were 7 major immunogenic bands at MW 98,000, 76,000, 68,000, 56,000, 52,000, 47,000, 42,000, and band 42,000 might be specific to S. mekongi. In S. mansoni, there were 11 major immunogenic bands at MW 98,000, 90,000, 76,000, 68,000, 56,000, 52,000, 47,000, 45,000, 31,000, 29,000, and 28,000; the bands at 31,000, 29,000 and 28,000 might be specific antigens for S. mansoni. When compared these immunogenic bands to lectin binding patterns, almost all immunogenic bands were labelled with at least two lectins and therefore they were all glycoproteins. Judging from the lectin binding patterns, these immunogenic bands appeared to be 2 groups: that is, the group of bands containing both internal (D-mannose/D-glucose and N-acetyl-D-glucosamine) and terminal sugar residues (D-galactose, N-acetyl-D-galactosamine and L-fucose) in their molecules. Another group of bands, especially 98,000, 68,000, which were the most prominent antigens, might contain principally the terminal sugar residues (D-galactose, N-acetyl-D-galactosamine and L-fucose). These sugar residues were evenly distributed on the membrane covering the upper half of ridges where the membrane turnover occurred. Therefore, these glycoproteins might be the major portion of the released antigens which would stimulate intense host immune response.
Description
Anatomy (Mahidol University 1989)
Degree Name
Master of Science
Degree Level
Master's degree
Degree Department
Faculty of Science
Degree Discipline
Anatomy
Degree Grantor(s)
Mahidol University