Silico identification, molecular characterization and expression analysis of the Trypanosoma brucei paraflagellar rod protein PFR3

Authors

  • M MORELL Departamento de Biología Molecular, Instituto de Parasitología y Biomedicina «López Neyra», CSIC. Granada
  • JL GARCÍA-PÉREZ Departamento de Biología Molecular, Instituto de Parasitología y Biomedicina «López Neyra», CSIC. Granada
  • MC THOMAS Departamento de Biología Molecular, Instituto de Parasitología y Biomedicina «López Neyra», CSIC. Granada
  • MC LÓPEZ Departamento de Biología Molecular, Instituto de Parasitología y Biomedicina «López Neyra», CSIC. Granada

Keywords:

Copy number, Gene, Leishmania, Molecular characterization, Paraflagellar rod protein, Silico identification, Trypanosoma brucei, Trypanosoma cruzi, Transcription

Abstract

In the present paper we describe the identification and isolation of the gene coding for T. brucei PFR3protein. The deduced amino acid sequence produces a protein of 592 residues with an isoelectric pointof 5.14 and shows a 68.9% sequence identity with T. cruzi PFR3 protein. However, the percentage ofhomology among T. brucei PFR3 and other available PFRs sequences from T. brucei and T. cruzi islower than 22%. In contrast to that described for members of paraflagellar rod protein family, thehighest divergence between T. cruzi and T. brucei PFR3 proteins is located at the central region of theprotein with a 38% of similarity over 200 amino acid. We estimate that there exist two copies of theT. brucei PFR3 protein per haploid genome. The gene is transcribed as a mRNA of approximately 3.6kb in length, equally abundant in both procyclic and bloodstream parasite forms.

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References

Hyams JS. The Euglena paraflagellar rod: structure, relationship to other flagellar components and preliminary biochemical

characterization. J Cell Sci 1982;55:199-210.

Cosson J, Cachon M, Cachon J, et al. Swimming behavior of the unicellular biflagellate Oxyrrhis marina: in vivo and in vitro movement of the two flagella. Biol Cell 1988;63:117-26.

Saborio JL, Manuel Hernandez J, Narayanswami S, et al. Isolation and characterization of paraflagellar proteins from Trypanosoma cruzi. J Biol Chem 1989;264:4071-5.

Bastin P, Pullen TJ, Moreira-Leite FF, et al. Inside and outside of the trypanosome flagellum: a multifunctional organelle.

Microbes Infect 2000;2:1865-74.

Maga JA, LeBowitz JH. Unravelling the kinetoplastid paraflagellar rod. Trends Cell Biol 1999;9: 409-13.

Woodward R, Cardewn MJ, Gull K. Molecular characterization of a novel, repetitive protein of the paraflagellar rod in Trypanosoma brucei. Mol Biochem Parasiol 1994;67:31-9.

Hunger-Glaser I, Seebeck T. Deletion of the genes for the paraflagellar rod protein PFR-A in Trypanosoma brucei is probably lethal. Mol Biochem Parasitol 1997;90:347-51.

Santrich C, Moore L, Sherwin T, et al. A motility function for the paraflagellar rod of Leishmania parasites revealed by PFR-2 gene knockouts. Mol Biochem Parasitol 1997;90:95-109.

Fouts DL, Stryker GA, Gorski KS, et al. Evidence for four distinct major protein components in the paraflagellar rod of Trypanosoma cruzi. J Biol Chem 1998;273:21846-55.

Wrightsman RA, Miller MJ, Saborio JL, et al. Pure paraflagellar rod protein protects mice against Trypanosoma cruzi infection. Infect Immun 1995;63:122-5.

Miller MJ, Wrightsman RA, Stryker GA, et al. Protection of mice against Trypanosoma cruzi by immunization with paraflagellar rod proteins requires T cell, but not B cell, function. J Immunol 1997;158:5330-7.

Luhrs KA, Fouts DL, Manning JE. Immunization with recombinant paraflagellar rod protein induces protective against

Trypanosoma cruzi infection. Vaccine 2003;21:3058-69.

Degrave WM, Melville S, Ivens A, Aslett M (2001) Parasite genome initiatives. Int J Parasitol 31:532-536.

Cross GAM. Identification, purification and properties of variant-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei. Parasitology. 1975;71:393-417.

Sambroock J, Maniatis T, Fritsh EF (1989) Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, U.S.A.

Sanger F, Nicklen S, Coulson AR. DNA sequencing with chain-terminating inhibitors. Proc Natl Acad Sci, USA 1977;74: 5463-7.

Deflorin J, Rudolf M, Seebeck T. The major components of the paraflagellar rod of Trypanosoma brucei are two similar, but distinct proteins which are encoded by two different gene loci. J Biol Chem 1994;269:28745-51.

Wrightsman RA, Luhrs KA, Fouts D, et al. Paraflagellar rod protein-specific CD8+ cytotoxic T lymphocytes target Trypanosoma cruzi-infected host cells. Parasite Immunol 2002;24:401-12.

Bringaud F, Garcia-Perez JL, Heras SR, et al. Identification of non-autonomous non-LTR retrotransposons in the genome of Trypanosoma cruzi. Mol Biochem Parasitol 2002;124:73-8.

Aguero F, Verdun RE, Frasch AC, et al. A random sequencing approach for the analysis of the Trypanosoma cruzi genome: general structure, large gene and repetitive DNA families, and gene discovery. Genome Res 2000;10:1996-2005.

Degrave WM, Melville S, Ivens A, et al. Parasite genome initiatives. Int J Parasitol 2001;31:532-6.

Marañón C, Puerta C, Alonso C, et al. Control mechanisms of the H2A genes expression in Trypanosoma cruzi. Mol Biochem Parasitol 1998;92:313-24.

Published

2004-12-20

How to Cite

1.
MORELL M, GARCÍA-PÉREZ J, THOMAS M, LÓPEZ M. Silico identification, molecular characterization and expression analysis of the Trypanosoma brucei paraflagellar rod protein PFR3. Ars Pharm [Internet]. 2004 Dec. 20 [cited 2024 May 21];46(1):73-84. Available from: https://revistaseug.ugr.es/index.php/ars/article/view/5065

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Original Articles