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1.
Mol Biochem Parasitol ; 71(1): 1-13, 1995 Apr.
Article in English | MEDLINE | ID: mdl-7630374

ABSTRACT

An abundant 11-kDa membrane protein was purified from African trypanosomes by organic solvent extraction and octyl-Sepharose chromatography. This protein cross-reacts with monoclonal antibodies originally generated against the lipophosphoglycan-associated protein of Leishmania donovani. Immunoblot analysis showed that the 11-kDa molecule was present in a variety of species of kinetoplastids. It was found in several species and subspecies of African trypanosomes and was present in low amounts in bloodstream forms and in larger amounts in procyclic, epimastigote and metacyclic life cycle stages. Expression of the 11-kDa molecule rapidly increased during transformation from bloodstream forms to procyclic forms, paralleling expression of the major surface glycoprotein of Trypanosoma congolense, the glutamic acid/alanine-rich protein, an analogue of T. brucei procyclin. The molecule was present in procyclic trypanosome membranes at approximately 2 x 10(5)-1 x 10(6) molecules per cell, suggesting it may have an important role in parasite membrane organization and function. Amino-acid analysis of the trypanosome 11-kDa protein showed it had a different composition than that of its leishmania counterpart. Its wide distribution in kinetoplastids and its membrane disposition suggest a name for this class of molecules: kinetoplastid membrane protein-11 (KMP-11).


Subject(s)
Kinetoplastida/chemistry , Membrane Glycoproteins/analysis , Protozoan Proteins/analysis , Trypanosoma/chemistry , Amino Acids/analysis , Animals , Antibodies, Monoclonal , Antibodies, Protozoan , Cell Membrane/parasitology , Cross Reactions , Kinetoplastida/growth & development , Membrane Glycoproteins/chemistry , Membrane Glycoproteins/immunology , Membrane Glycoproteins/isolation & purification , Molecular Weight , Protozoan Proteins/chemistry , Protozoan Proteins/immunology , Protozoan Proteins/isolation & purification , Trypanosoma/growth & development
2.
Infect Immun ; 62(11): 4893-9, 1994 Nov.
Article in English | MEDLINE | ID: mdl-7927770

ABSTRACT

Kinetoplastid membrane protein 11 (KMP-11) from Leishmania donovani is an abundant 11-kDa surface membrane glycoprotein. Lymph node cells from mice of six different H-2 haplotypes immunized with KMP-11 or with L. donovani promastigotes were stimulated to proliferate in vitro KMP-11. Primed purified T cells required antigen presentation since they were not stimulated unless KMP-11-pulsed or L. donovani-infected macrophages were added. Promastigotes of a wide variety of Leishmania species and procyclic forms of African trypanosomes stimulated proliferation of KMP-11-primed or L. donovani promastigote-primed lymph node cells. All of the Leishmania promastigotes and African trypanosomes tested contained an 11-kDa protein, as detected by immunoblotting with KMP-11-specific monoclonal antibodies. The widespread distribution of the 11-kDa (KMP-11) molecules and their ability to stimulate strong T-lymphocyte proliferation in a non-H-restricted fashion suggest that they may be important molecules for induction of cell-mediated immune responses.


Subject(s)
Antigens, Protozoan/immunology , Leishmania donovani/immunology , Membrane Glycoproteins/immunology , Protozoan Proteins/immunology , T-Lymphocytes/immunology , Animals , Antigen-Presenting Cells/immunology , Glycosphingolipids/immunology , Interleukin-2/biosynthesis , Lymphocyte Activation , Macrophages/immunology , Mice , Mice, Inbred Strains
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