Hostname: page-component-7dd5485656-wjfd9 Total loading time: 0 Render date: 2025-10-31T14:54:56.217Z Has data issue: false hasContentIssue false
  • English
  • Français

Cytoskeleton-associated antigens from African trypanosomes are recognized by self-reactive antibodies of uninfected mice

Published online by Cambridge University Press:  06 April 2009

N. Müller ,
M. Imboden ,
E. Detmer ,
J. M. Mansfield  and
T. Seebeck
N. Müller
Affiliation:
Institut für Allgemeine Mikrobiologie, University of Bern, Baltzerstrasse 4, CH-3012 Bern, Switzerland
M. Imboden
Affiliation:
Institut für Allgemeine Mikrobiologie, University of Bern, Baltzerstrasse 4, CH-3012 Bern, Switzerland
E. Detmer
Affiliation:
Institut für Allgemeine Mikrobiologie, University of Bern, Baltzerstrasse 4, CH-3012 Bern, Switzerland
J. M. Mansfield
Affiliation:
Department of Animal Health and Biomedical Sciences, 1655 Linden Drive, University of Wisconsin, Madison, WI 53706, USA
T. Seebeck
Affiliation:
Institut für Allgemeine Mikrobiologie, University of Bern, Baltzerstrasse 4, CH-3012 Bern, Switzerland
Get access Rights & Permissions [Opens in a new window]

Summary

Serum from uninfected mice of different strains, as well as from germ-free animals, contains antibodies which react specifically with at least two trypanosomal proteins, I/6 and MARP1. These antibody populations are highly specific for the respective proteins, are of similar affinity as hyperimmune antibodies, and consist of IgM as well as IgG isotypes. Hyperimmune antibody raised against the cross-reacting trypanosomal protein I/6 detects a 60 kDa protein in mouse 3T6 cells, which is a component of the fibroblast cytoskeleton.

Keywords

cytoskeletal-associated antigensAfrican trypanosomesantibody response

Information

Type
Research Article
Information
Parasitology , Volume 107 , Issue 4 , November 1993 , pp. 411 - 417
Copyright
Copyright © Cambridge University Press 1993

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.)

Article purchase

Temporarily unavailable

References

REFERENCES

Bancroft, G. J. & Askonas, B. A. (1985). Immunobiology of African trypanosomiasis in laboratory rodents. In Immunology and Pathogenesis of Trypanosomiasis (ed. Tizard, I.), pp. 75–101. Boca Raton, Florida: CRC Press.Google Scholar
Burgess, D. E. & Jerrells, T. (1985). Molecular identity and location of invariant antigens on Trypanosoma brucei rhodesiense defined with monoclonal antibodies reactive with sera from trypanosomiasis patients. Infection and Immunity 50, 893–9.CrossRefGoogle Scholar
Cross, G. A. M. (1990). Cellular and genetic aspects of antigenic variation in trypanosomes. Annual Review of Immunology 8, 83–116.CrossRefGoogle ScholarPubMed
De Gee, A. L. W., Levine, R. F. & Mansfield, J. M. (1988). Genetics of resistance to the African trypanosomes. VI. Heredity of resistance and variable glycoprotein specific immune responses. J. Immunol. 140, 283–8.CrossRefGoogle Scholar
Hemphill, A., Affolter, M. & Seebeck, T. (1992). A novel microtubule-binding motif identified in a high molecular weight microtubule-associated protein from Trypanosoma brucei. Journal of Cell Biology 117, 95–103.CrossRefGoogle Scholar
Hemphill, A., Seebeck, T. & Lawson, D. (1991). The Trypanosoma brucei cytoskeleton: ultrastructure and localization of microtubule-associated and spectrinlike proteins using quick-freeze, deep-etch immunogold electron microscopy. Journal of Structural Biology 107, 211–20.CrossRefGoogle ScholarPubMed
Morrison, W. I., Murray, M. & Akol, G. W. O. (1985). Immune responses of cattle to African trypanosomes. In Immunology and Pathogenesis of Trypanosomiasis (ed. Tizard, I.), pp. 103–31. Boca Raton, Florida: CRC Press.Google Scholar
Müller, N., Hemphill, A., Imboden, M., Duvallet, G., Dwinger, R. H. & Seebeck, T. (1992). Identification and characterization of two repetitive non-variable antigens from African trypanosomes which are recognized early during infection. Parasitology 104, 111–19.CrossRefGoogle ScholarPubMed
Schlaeppi, K., Deflorin, J. & Seebeck, T. (1989). The major component of the paraflagellar rod of Trypanosoma brucei is a helical protein that is encoded by two identical, tandemly linked genes. Journal of Cell Biology 109, 1695–709.CrossRefGoogle ScholarPubMed
Schneider, A., Hemphill, A. & Seebeck, T. (1988). Large microtubule-associated protein of T. brucei has tandemly repeated, near-identical sequences. Science 241, 459–62.CrossRefGoogle ScholarPubMed
Shapiro, S. Z. & Murray, M. (1982). African trypanosome antigens recognized during the course of infection in N'dama and Zebu cattle. Infection and Immunity 35, 410–16.CrossRefGoogle ScholarPubMed
Shapiro, S. Z. & Pearson, T. W. (1986). African trypanosomiasis: antigens and host-parasite interactions. In Parasite Antigens (ed. Pearson, T. W.), pp. 215–274. New York: Marcel Dekker.Google Scholar
Theodos, C. M. & Mansfield, J. M. (1990). Regulation of B cell responses to the variant surface glycoprotein molecule in trypanosomiasis. II. Down-regulation of idiotype expression is associated with the appearance of lymphocytes expressing antiidiotypic receptors. Journal of Immunology 144, 4022–9.CrossRefGoogle Scholar
Vogel, M., Müller, N., Gottstein, B. & Seebeck, T. (1988). Production of recombinant antigen of Echinococcus multilocularis with high immunodiagnostic sensitivity and specificity. Molecular and Biochemical Parasitology 31, 117–26.CrossRefGoogle ScholarPubMed