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Infection and Immunity, February 2000, p. 848-860, Vol. 68, No. 2
Laboratory of Molecular Parasitology, IBMM,
Free University of Brussels ULB, 6041 Gosselies,1 Laboratory of Cellular
Immunology, Flanders Interuniversity Institute for Biotechnology
Received 2 July 1999/Returned for modification 31 August
1999/Accepted 28 October 1999
During Trypanosoma brucei infections, the response
against the variant surface glycoprotein (VSG) of the parasite
represents a major interaction between the mammalian host immune system
and the parasite surface. Since immune recognition of other parasite derived factors also occurs, we examined the humoral host response against trypanosome heat shock protein 60 (HSP60), a conserved antigen
with an autoimmune character. During experimental T. brucei infection in BALB/c mice, the anti-HSP60 response was induced when
parasites differentiated into stumpy forms. This response was
characterized by a stage-specific immunoglobulin isotype switching as
well as by the induction of an autoimmune response. Specific recognition of trypanosome HSP60 was found to occur during the entire
course of infection. Immunoglobulin G2a (IgG2a) and IgG2b antibodies,
induced mainly in a T-cell-independent manner, were observed during the
first peak of parasitemia, whereas IgG1 and IgG3 antibodies were found
at the end of the infection, due to a specific T-cell-mediated
response. Comparative analysis of the kinetics of anti-HSP60,
anti-invariant surface glycoprotein 70 (ISG70), and anti-VSG antibody
responses indicated that the three trypanosome antigens give rise to
specific and independent patterns of immunoglobulin isotype switching.
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Comparative Analysis of Antibody Responses against
HSP60, Invariant Surface Glycoprotein 70, and Variant Surface
Glycoprotein Reveals a Complex Antigen-Specific Pattern of
Immunoglobulin Isotype Switching during Infection by
Trypanosoma brucei
Free
University of Brussels VUB, 1640 Sint Genesius
Rode,2 and Department of Biological
Chemistry, Faculty of Science, University of Mons-Hainaut, 7000 Mons,3 Belgium
*
Corresponding author. Mailing address: Laboratory of
Molecular Parasitology, IBMM, Free University of Brussels, Rue des
Professeurs Jeener et Brachet 12, 6041 Gosselies, Belgium. Phone:
32-2-650.97.59. Fax: 32-2-650.97.50. E-mail:
mradwans{at}dbm.ulb.ac.be.
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