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Infection and Immunity, November 2001, p. 6776-6784, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6776-6784.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Biochemical and Biological Characterization of the Protective Leishmania pifanoi Amastigote Antigen P-8

M. Colmenares,1 M. Tiemeyer,2 P. Kima,1,dagger and D. McMahon-Pratt1,*

Departments of Epidemiology and Public Health1 and Cell Biology,2 Yale University School of Medicine, New Haven, Connecticut

Received 23 October 2000/Returned for modification 13 December 2000/Accepted 23 July 2001

The Leishmania pifanoi amastigote antigen P-8 has been previously shown to induce protective immunity in a murine model of cutaneous leishmaniasis (L. Soong, S. M. Duboise, P. Kima, and D. McMahon-Pratt, Infect. Immun. 63:3559-3566, 1995). As this antigen is of interest for further vaccine studies, the biochemical characterization of P-8 was undertaken. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Western-blot analysis, and gel filtration chromatography revealed that P-8 antigen consisted of two proteoglycolipid complexes. The P-8 epitope is associated with the L. pifanoi amastigote-specific glycolipid components found in the two complexes. The P-8 complex 1 (P-8c1) consists of a 56-kDa serine metalloproteinase, apolipoprotein E (derived from fetal bovine serum), and amastigote-specific glycolipids. The P-8 complex 2 (P-8c2) consists of a 31-kDa cysteine proteinase associated with amastigote glycolipids. Biochemical analyses suggest that the P-8 antigenic glycolipids may be distinct from previously described Leishmania glycolipids (glycosylinositolphospholipids and sphingoglycolipids). Protective immunity studies revealed that P-8c1 (serine metalloproteinase-glycolipid complex) confers comparable protection against infection as immunopurified P-8. The isolated P-8c2 (cysteine proteinase-glycolipid complex) does not provide significant protection, nor does stimulation with P-8c2 result in significant T-cell activation in P-8- or P-8c2-vaccinated mice. Consequently, the P-8c1 complex appears to be the immunodominant component of P-8.

* Corresponding author. Mailing address: Yale University School of Medicine, Department of Epidemiology and Public Health, P.O. Box 208034, 60 College St., New Haven, CT 06510-8034. Phone: (203) 785-4481. Fax: (203) 737-2921. E-mail: diane.mcmahon-pratt{at}yale.edu.

dagger Present address: Department of Microbiology and Cell Science, University of Florida, Gainesville, FL 32611-0700.

Infection and Immunity, November 2001, p. 6776-6784, Vol. 69, No. 11
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.11.6776-6784.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Whitaker, S. M., Colmenares, M., Pestana, K. G., McMahon-Pratt, D. (2008). Leishmania pifanoi Proteoglycolipid Complex P8 Induces Macrophage Cytokine Production through Toll-Like Receptor 4. Infect. Immun. 76: 2149-2156 [Abstract] [Full Text]  
  • Colmenares, M., Kima, P. E., Samoff, E., Soong, L., McMahon-Pratt, D. (2003). Perforin and Gamma Interferon Are Critical CD8+ T-Cell-Mediated Responses in Vaccine-Induced Immunity against Leishmania amazonensis Infection. Infect. Immun. 71: 3172-3182 [Abstract] [Full Text]  


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