scholarly journals Synthesis of the Carbohydrate Moiety of Glycoproteins from the Parasite Echinococcus granulosus and Their Antigenicity against Human Sera

Molecules ◽  
2021 ◽  
Vol 26 (18) ◽  
pp. 5652
Author(s):  
Noriyasu Hada ◽  
Tokio Morita ◽  
Takashi Ueda ◽  
Kazuki Masuda ◽  
Hiromi Nakane ◽  
...  
Keyword(s):  
Echinococcus Granulosus ◽  
Immunosorbent Assay ◽  
Cystic Echinococcosis ◽  
Alveolar Echinococcosis ◽  
Total Yield ◽  
Carbohydrate Moiety ◽  
Enzyme Linked Immunosorbent Assay ◽  
Human Sera

Stereocontrolled syntheses of biotin-labeled oligosaccharide portions containing the carbohydrate moiety of glycoprotein from Echinococcus granulosus have been accomplished. Trisaccharide Galβ1-3Galβ1-3GalNAcα1-R (A), tetrasaccharide Galα1-4Galβ1-3Galβ1-3GalNAcα1-R (B), and pentasaccharide Galα1-4Galβ1-3Galβ1-3Galβ1-3GalNAcα1-R (C), (R = biotinylated probe) were synthesized by stepwise condensation and/or block synthesis by the use of 5-(methoxycarbonyl)pentyl 2-azido-4,6-O-benzylidene-2-deoxy-α-d-galactopyranoside as a common glycosyl acceptor. The synthesis of the tetrasaccharide and the pentasaccharide was improved from the viewpoint of reducing the number of synthetic steps and increasing the total yield by changing from stepwise condensation to block synthesis. Moreover, hexasaccharide E, which contains the oligosaccharide sequence which occurs in E. granulosus, was synthesized from trisaccharide D. We examined the antigenicity of these five oligosaccharides by an enzyme-linked immunosorbent assay (ELISA). Although compounds of C–E did not exhibit antigenicity against cystic echinococcosis (CE) patient sera, compounds B, D, and E showed good serodiagnostic potential for alveolar echinococcosis (AE).

Serodiagnostic potential of chemically synthesized glycosphingolipid antigens in an enzyme-linked immunosorbent assay for alveolar echinococcosis

2006 ◽  
Vol 80 (4) ◽  
pp. 387-391 ◽  
Author(s):  
K. Yamano ◽  
N. Hada ◽  
T. Yamamura ◽  
T. Takeda ◽  
H. Honma ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Immunosorbent Assay ◽  
Echinococcus Multilocularis ◽  
Cystic Echinococcosis ◽  
Alveolar Echinococcosis ◽  
Carbohydrate Antigen ◽  
Single Component ◽  
Enzyme Linked Immunosorbent Assay ◽  
Protein Antigens ◽  
Specific Reactions

AbstractIn the serodiagnosis of alveolar echinococcosis, the detection of specific reactions against not only protein but also carbohydrate antigen is useful and both antigens supplement each other. Though recombinant protein antigens have recently advanced, the preparation of carbohydrate antigen still depends on extraction from crude antigens. In the latter case, it is not conventional to obtain carbohydrate antigen as a single component for examination and research. Therefore, chemically synthesized carbohydrate antigens were prepared for serodiagnosis by the enzyme-linked immunosorbent assay (ELISA). Four antigens with the structure of glycosphingolipids fromEchinococcus multiloculariswere examined and one antigen, Galβ1-6(Fucα1-3)Galβ1-6Galβ1-ceramide, was found to show significant serodiagnostic potential in differentiating alveolar from cystic echinococcosis.

scholarly journals Enzyme-Linked Immunosorbent Assay To Differentiate the Antibody Responses of Animals Infected with Brucella Species from Those of Animals Infected with Yersinia enterocolitica O9

2003 ◽  
Vol 10 (4) ◽  
pp. 710-714 ◽  
Author(s):  
Janchivdorj Erdenebaatar ◽  
Balgan Bayarsaikhan ◽  
Masahisa Watarai ◽  
Sou-ichi Makino ◽  
Toshikazu Shirahata
Keyword(s):  
Yersinia Enterocolitica ◽  
Immunosorbent Assay ◽  
Brucella Abortus ◽  
Field Trial ◽  
Antibody Responses ◽  
Enzyme Linked Immunosorbent Assay ◽  
Brucella Species ◽  
Serological Tests ◽  
Human Sera ◽  
Immunosorbent Assays

ABSTRACT Enzyme-linked immunosorbent assays using antigens extracted from Brucella abortus with n-lauroylsarcosine differentiated natural Brucella-infected animals from Brucella-vaccinated or Yersinia enterocolitica O9-infected animals. A field trial in Mongolia showed cattle, sheep, goat, reindeer, camel, and human sera without infection could be distinguished from Brucella-infected animals by conventional serological tests.

scholarly journals Sensitive Enzyme-Linked Immunosorbent Assay for Detection of Antibodies Against Typhus Rickettsiae, Rickettsia prowazekii and Rickettsia typhi

1977 ◽  
Vol 6 (2) ◽  
pp. 101-110
Author(s):  
Sidney Halle ◽  
Gregory A. Dasch ◽  
Emilio Weiss
Keyword(s):  
Immunosorbent Assay ◽  
Complement Fixation ◽  
Differential Susceptibility ◽  
Immunoglobulin M ◽  
Enzyme Linked Immunosorbent Assay ◽  
Rickettsia Prowazekii ◽  
Rickettsia Typhi ◽  
Titration Curves ◽  
Ether Extraction ◽  
Human Sera

An enzyme-linked immunosorbent assay (ELISA) has been developed for the titration of rickettsial antibodies in human and animal sera. Two preparations of soluble typhus-group antigens were obtained from Rickettsia typhi and Rickettsia prowazekii by ether extraction: a standard antigen from infected yolk sacs (YS antigen) and one free of yolk sac contaminants from Renografin-purified rickettsiae (PR antigen). Rabbit, mouse, and guinea pig sera were obtained by immunization with viable purified R. typhi or R. prowazekii . Human sera were obtained from individuals who had recovered from laboratory infections with either typhus rickettsia months or years previously. Goat-derived anti-immunoglobulins were conjugated to alkaline phosphatase with glutaraldehyde. Although the PR and YS antigens gave equivalent antibody titers in the complement fixation test, the PR antigen was clearly superior in the ELISA. With this antigen, the titration curves of all antisera were linear over a wider range of serum concentrations and the titers were higher than with the YS antigen. With YS and PR antigens, ELISA titers were higher than those obtained by complement fixation by one and two orders of magnitude, respectively. In human sera, immunoglobulin G and immunoglobulin M antibodies were demonstrated by their respective anti-immunoglobulins and by differential susceptibility to ethanethiol. ELISA titers showed some type specificity, whereas none was observed in complement fixation tests. The ELISA is highly sensitive, reproducible, and easily adaptable to the various requirements of clinical and research laboratories.

Sign in / Sign up

Export Citation Format

Share Document