Hostname: page-component-586b7cd67f-2brh9 Total loading time: 0 Render date: 2024-11-26T21:45:08.575Z Has data issue: false hasContentIssue false

Antigenic relationships among Trypanosoma lewisi—complex cells*

I. Agglutinins in antisera

Published online by Cambridge University Press:  06 April 2009

David Richard Lincicome
Affiliation:
Laboratory of Parasitology, Department of Zoology, Howard University, Washington, D.C.
Roy Chester Watkins
Affiliation:
Laboratory of Parasitology, Department of Zoology, Howard University, Washington, D.C.

Extract

Cells of six isolates of Trypanosoma lewisi from the United States, England, Puerto Rico, Costa Rica, and Singapore were matched against antiserum to the ‘L’ isolate in microagglutinin chambers. Antisera were prepared in Sprague-Dawley rats. Serum protein determinations were made by the biuret reaction; electrophoretic fractionations of serum proteins were done with a semi-closed horizontal system (Evans & Stirewalt, 1947) at 4°C for 24 h, 120 V, and 8 mA with paper strips. Electrolyte was veronal buffer, pH 8·6 and μ 0·058. Agglutinin absorptions were carried out using inactivated anti-‘L’ sera.

Total protein (mg/ml) values were higher in all infected animals (60 vs. 54). Albumin values (%) were higher in controls (47 vs. 40);α-1 fractions were essentially unchanged (15%) as were α-2 values (6%). β Fractions were elevated in infected groups (21 vs. 17%), as were the γ globulins (19 vs. 12%).

Three protocols employing agglutinin reactions were completed. In two protocols 3+ agglutinin end-points were obtained with four isolates using 1·45–1·47 μg of immune γ globulin. Two of the isolates (Puerto Rico and Singapore) required 10 times this amount of immune globulin for the same end-point. In two other tests all isolates gave reaction end-points that required greater quantities (by a factor of ca. 500) of immune γ globulin than obtained in the first two tests, and there was further evidence that the Costa Rican isolate was quantitatively different from the others. These facts are interpreted to mean that all six geographic isolates show close qualitative relationships to each other, but that the relationships for the Puerto Rican, Singapore and Costa Rican isolates are quantitatively different. Agglutinins could not be absorbed from immune serum by any of the cells.

Type
Research Article
Copyright
Copyright © Cambridge University Press 1965

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

Borsos, T. & Kent, H. N. (1958). Serum gamma globulin and Trypanosoma cruzi agglutinin in embryonic normal and germ-free chickens. Proc. Soc. Exp. Biol., N.Y., 99, 105–8.CrossRefGoogle ScholarPubMed
Chandler, A. C. (1958). Some considerations on the nature of immunity in Trypanosoma lewisi infections. J. Parasit. 44, 129–35.CrossRefGoogle ScholarPubMed
Cunningham, M. P. & Vickerman, K. (1962). Antigenic analysis in the Trypanosoma brucei group using the agglutination reaction. Trans. r. Soc. trop. Med. Hyg. 56, 4859.CrossRefGoogle ScholarPubMed
Evans, A. S. & Stirewalt, M.A. (1957). Serologic reactions in Schistosoma mansoni infections. II. Ionographic fractionation of sera of mice with progressive disease. Expl Parasit. 6, 817.CrossRefGoogle Scholar
Gornall, A. G., Bardawill, C. J. & David, M. M. (1949). Determination of serum proteins by means of the biuret reaction. J. biol. Chem. 177, 751–66.CrossRefGoogle ScholarPubMed
Gray, A. R. (1961). Precipitation in agar gel in the study of antigen antibody reactions in African trypanosomiasis. Ann. trop. Med. Parasit. 55, 142.Google Scholar
Kingsley, G. B. (1939). The determination of serum total protein by biuret reaction. J. biol. Chem. 131, 197200.CrossRefGoogle Scholar
Lincicome, D. R. & Hill, G. C. (1965). Oxygen consumption of Trypanosoma lewisi complex cells. 1. ‘L’ isolate. Comp. Biochem. Physiol. in press.Google Scholar
Lincicome, D. R. & Watkins, R. C. (1963 a). Method of preparing pure cell suspensions of Trypanosoma lewisi. A.I.B.S. Bull. 13, 53–4.Google Scholar
Lincicome, D. R. & Watkins, R. C. (1963 b). Relationship of several isolates of Trypanosoma lewisi shown by agglutinin titers. J. Parasit. 49, 57–8.Google Scholar
Norman, L. & Kagan, I. G. (1960). Immunologic studies on Trypanosoma cruzi. II. Acquired immunity in mice infected with avirulent American strains of T. cruzi. J. infect. Dis. 107, 168–74.CrossRefGoogle ScholarPubMed
Soltys, M. A. (1957 a). Immunity in trypanosomiasis. I. Neutralization reaction. Parasitology, 47, 375–89.CrossRefGoogle ScholarPubMed
Soltys, M. A. (1957 b). Immunity in trypanosomiasis. II. Agglutination reaction with African trypanosomes. Parasitology, 47, 390–5.CrossRefGoogle ScholarPubMed
Taliaferro, W. H. (1932). Trypanocidal and reproduction inhibiting antibodies to Trypanosoma lewisi in rats and rabbits. Amer. J. Hyg. 16, 3284.Google Scholar
Tate, P. (1951). Antagonism of Spirillum minus infections in rats towards Trypanosoma lewisi and T. equinum. Parasitology, 41, 117–27.CrossRefGoogle Scholar
Thillet, C. & Chandler, A. C. (1957). Immunization against Trypanosoma lewisi in rats by injections of metabolic products. Science, 125, 346–7.CrossRefGoogle Scholar