Fractionation of mycobacterial integral membrane proteins by continuous elution SDS-PAGE reveals the immunodominance of low molecular weight subunits for human T cells

Clinical and Experimental Immunology

Volumn 109, Issue 3, 1997, Pages 446-450

  Mehrotra, J ^b   Mittal, A ^b   Dhindsa, M S ^a   Sinha, S ^b  

^a BASE HOSPITAL   (India)

^b CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

Continuous elution SDS PAGE; Human T cell proliferation; Integral membrane proteins; Mycobacterium; Mycobacterium fortuitum

Indexed keywords

CALNEXIN; MYCOBACTERIUM ANTIGEN;

ARTICLE; CELL PROLIFERATION; HUMAN; HUMAN CELL; IMMUNE RESPONSE; LYMPHOCYTE PROLIFERATION; MYCOBACTERIUM FORTUITUM; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PURIFICATION; T LYMPHOCYTE; T LYMPHOCYTE ACTIVATION; T LYMPHOCYTE SUBPOPULATION; TUBERCULOID LEPROSY;

EID: 0030801701     PISSN: 00099104     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2249.1997.4531351.x     Document Type: Article

References (26)

1. Kaufmann SHE. Immunity against intracellular bacteria: biological effector functions and antigen specificity of T lymphocytes. Curr Topics Microbiol Immunol 1988; 138:141-76.
2. Young DB, Kaufmann SHE, Hermans PWM, Thole JER. Mycobacterial protein antigens: a compilation. Mol Microbiol 1992; 6:133-45.
3. Thole JER, Wieles V, Clark-Curtiss JE, Ottenhoff THM, Rinke de Wit TF. Immunological and functional characterisation of Mycobacterium leprae protein antigens: an overview. Mol Microbiol 1995; 18:790-800.
4. Abou-Zeid C, Filley E, Steele J, Rook GAW. A simple new method for using antigens separated by polyacrylamide gel electrophoresis to stimulate lymphocytes in vitro after converting bands cut from Western blots into antigen bearing particles. J Immunol Methods 1987; 98:5-10.
5. Gulle H, Schoel B, Kaufmann SHE. Direct blotting with viable cells of protein mixtures separated by two-dimensional gel electrophoresis. J Immunol Methods 1990; 133:253-61.
6. Andersen P, Heron I. Simultaneous electroelution of whole SDS-polyacrylamide gels for the direct cellular analysis of complex protein mixtures. J Immunol Methods 1993; 161:29-39.
7. Mountford AP, Wilson RA. Fractionation of schistosome antigens by high-performance elecrophoretic chromatography and their screening for the ability to induce Th1 lymphocyte activity. J Immunol Methods 1993; 160:237-44.
8. Mehrotra J, Bisht D, Tiwari VD, Sinha S. Serological distinction of integral plasma membrane proteins as a class of mycobacterial antigens and their relevance for human T cell activation. Clin Exp Immunol 1995; 102:626-34.
9. Ottenhoff THM, Converse PJ, Gebre N, Wondimu A, Ehrenberg JP, Kiessling R. T cell responses to fractionated Mycobacterium leprae antigens in leprosy. The lepromatous non-responder defect can be overcome in vitro by stimulation with fractionated M. leprae components. Eur J Immunol 1989; 19:707-13.
10. Ridley DS, Jopling WH. Classification of leprosy according to immunity: a five group system. Int J Lepr 1966; 34:255-73.
11. Bordier C. Phase separation of integral membrane proteins in Triton X-114 solution. J Biol Chem 1981; 256:1604-7.
12. Markwell MAK, Haas SM, Bieber LL, Tolbert NE. A modification of the Lowry procedure to simplify protein determination in membrane and lipoprotein samples. Anal Biochem 1978; 87:206-10.
13. Leammli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 1970; 227:680-5.
14. Wray W, Boulikas T, Wray VP, Hancock R. Silver staining of proteins in polyacrylamide gels. Anal Biochem 1981; 118:197-203.
15. Wessel D, Flügge UI. A method for the quantitative recovery of protein in dilute solution in the presence of detergents and lipids. Anal Biochem 1984; 138:141-3.
16. Arand M, Friedberg T, Oesch F. Colorimetric quantitation of trace amounts of sodium lauryl sulfate in the presence of nucleic acids and proteins. Anal Biochem 1992; 207:73-75.
17. Fountoulakis M, di Lorenzo ET, Juranville JF, Mannberg M. Purification of interferon γ-interferon γ receptor complexes by preparative electrophoresis on native gels. Anal Biochem 1993; 208:270-6.
18. Harwig SSL, Chen NP, Park ASK, Lehrer RI. Purification of cysteine rich bioactive peptides from leukocytes by a continuous acid-urea polyacrylamide gel electrophoresis. Anal Biochem 1993; 208: 382-6.
19. Boesen H, Jensen BN, Wilcke T, Andersen P. Human T cell response to secreted antigen fractions of Mycobacterium tuberculosis. Infect Immun 1995; 63:1491-7.
20. Sinha S, Sreevatsa, Gupta SK, Sengupta U. A comparative study of immunising and delayed hypersensitivity eliciting antigens of Mycobacterium leprae, M. tuberculosis, M. vaccae and M. bovis (BCG). Int J Lepr 1987; 55:42-53.
21. Germain RN. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell 1994; 76:287-99.
22. Young DB, Garbe TR. Lipoprotein antigens of Mycobacterium tuberculosis. Res Microbiol 1991; 142:55-65.
23. Akins DR, Purcell BK, Mitra MM, Norgard MV, Radolf JD. Lipid modification of the 17 kilodalton membrane immunogen of Treponema pallidum determines macrophage activation as well as amphiphilicity. Infect Immun 1993; 61:1202-10.
24. Hammer J, Valsanini P, Tolba K, Bolin D, Higelin J, Takacs B, Sinigaglia F. Promiscuous and allele specific anchors in HLA-DR binding peptides. Cell 1993; 74:197-203.
25. Deres KH, Schild H, Wiesmuller K-H, Jung G, Rammensee HG. In vivo priming of virus specific cytotoxic T lymphocytes with synthetic lipopeptide vaccine. Nature (London) 1989; 342:561-4.
26. Chamberlain NR, Brandt ME, Erwin AL, Radolf JD, Norgard MV. Major integral membrane protein immunogens of Treponema pallidum are proteolipids. Infect Immun 1989; 57:2872-7.