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Genes coding structural proteins in the Leishmania braziliensis complex.

C Padilla1, T Barreto, M De Los Santos

  • 1Instituto Nacional de Salud, Centro Nacional de Laboratorios de Salud Pública, Jr Capac Yupanqui 1400, Jesus Maria, Lima, Perú.

Transactions of the Royal Society of Tropical Medicine and Hygiene
|June 12, 2002
PubMed
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This study identifies acidic ribosomal P proteins and histone H3 in Leishmania braziliensis for the first time. Despite mutations, P proteins likely retain ribosomal stalk function, with conserved histone H3 structure.

Area of Science:

  • Molecular Biology
  • Parasitology
  • Genetics

Background:

  • Acidic ribosomal P proteins and histone H3 are crucial for cellular function.
  • Leishmania braziliensis is a significant human pathogen.
  • Characterization of ribosomal proteins and histones in Leishmania species is ongoing.

Purpose of the Study:

  • To report the identification and initial characterization of acidic ribosomal P1 and P2b proteins and histone H3 in Leishmania braziliensis.
  • To investigate the potential structural and functional conservation of these proteins despite observed genetic variations.
  • To predict the three-dimensional structures of these proteins.

Main Methods:

  • Deoxyribonucleic acid (DNA) analysis and multiple sequence alignment were employed.

Related Experiment Videos

  • Amino acid sequences were deduced and compared with homologous proteins from other species.
  • Bioinformatic tools were used for predicting tridimensional structures.

    • Main Results:

    • Acidic ribosomal P1 and P2b proteins and histone H3 were identified in Leishmania braziliensis.
    • High mutation rates were detected in P proteins, but they likely maintain structural function in the ribosomal stalk.
    • Significant sequence identity was observed between Leishmania braziliensis histone H3 and homologous proteins from other species, with a divergent N-terminal end.
    • The deduced amino acid sequences showed identities of 51% (P1) and 61% (P2b) with Trypanosoma cruzi counterparts.
    • Histone H3 exhibited 82% and 70% identity with Leishmania infantum and T. cruzi histone H3, respectively.

    Conclusions:

    • The study provides the first report of acidic ribosomal P proteins and histone H3 in Leishmania braziliensis.
    • These proteins appear to be evolutionarily conserved, suggesting functional importance.
    • The findings contribute to understanding the molecular mechanisms of Leishmania parasites and offer potential targets for therapeutic intervention.