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Biochemical evidence of the antigenic cell surface heterogeneity ofLeishmania mexicana

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Abstract

In the present study, an enzymatical and structural analysis ofLeishmania mexicana cell-surface components was carried out, demonstrating that protease and acid phosphatase activities were present at theL. mexicana cell surface. These findings correlate with the expression of the main components detected on the surface ofL. mexicana promastigotes: the 50-kDa component is responsible for the acid phosphatase activity, whereas glycoprotein 65 (gp65) was characterized as the structural polypeptide of the surface protease. Furthermore, the 50- and 65-kDa antigens were found to be structurally different, inasmuch as no homology was observed in their peptide digestion profiles. The results presented in this communication confirm heterogeneity in the expression of the surface components ofL. mexicana promastigotes at both the structural and the biochemical level.

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Author notes

  1. Stephane Manenti

    Present address: Institut Jacques Monod, Centre National de la Recherche Scientifique (CNRS), Université Paris VII, 75251, Paris Cédex 05, France

Authors and Affiliations

  1. School of Biology, Faculty of Sciences, Central University of Venezuela, Apartado 47069, Los Chaguaramos, 1041, Caracas, Venezuela

    Stephane Manenti, Shirley Kutner, Ana Rascon & Angel G. Hernández

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  1. Stephane Manenti
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  2. Shirley Kutner
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  3. Ana Rascon
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  4. Angel G. Hernández
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Manenti, S., Kutner, S., Rascon, A. et al. Biochemical evidence of the antigenic cell surface heterogeneity ofLeishmania mexicana . Parasitol Res 76, 301–305 (1990). https://doi.org/10.1007/BF00928183

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