Characterization of plasma menbrane polypeptides of trypanosoma from bats

Pinho, Rosa Teixeira de; De-Simone, Salvatore Giovanni

doi:10.1590/s0074-02761989000100004

Cited by 6 publications

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“…Integral membrane proteins have a hydrophobic domain that interacts with the hydrophobic core of the lipid bilayer and, as a result, these proteins are recovered in the hydrophobic (detergent) phase (Bordier 1981). This procedure has been used for the extraction of proteins from protozoa such as Leishmania (Murray et al 1989), Toxoplasma gondii (Giovanni de Simone et al 1988b), Crithidia and various T. cruzi strains (Giovanni de Simone et al 1987, 1988a and trypanosomatids from bats (Pinho and Giovanni de Simone 1989). In the present study, each of the T. cruzi G and Y strains as well as clone Dm28c exhibited a characteristic strain-specific distribution of proteins.…”

Section: Discussionmentioning

confidence: 99%

Glycolipid and protein profiles in trypanosomatids

et al. 1994

Parasitol Res

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A comparative study of glycolipid and protein composition in Trypanosoma cruzi and non-pathogenic trypanosomatids was carried out using Triton X-114 extraction. Protein profiles were analysed by polyacrylamide gel electrophoresis in sodium dodecyl sulphate (SDS-PAGE), and glycolipids were detected using high-performance thin-layer chromatography (HPTLC). Hydrophilic protein profiles were similar in non-pathogenic protozoa. Endotrypanum schaudinni, Crithidia luciliae and T. mega showed five characteristic protein bands ranging between 30 and 66 kDa. In the hydrophobic phase, a band of 50 kDa was present only in T. mega. Strain-specific protein distribution was detected in T. cruzi clone Dm28c and T. cruzi G and Y strains; clone Dm28c had five typical hydrophilic proteins at between 24 and 45 kDa, the G strain had two bands at 45 kDa in the hydrophilic phase and the Y strain had a major protein band at 24 kDa in both phases. T. dionisii and T. cruzi clone Dm28c showed a characteristic distribution of three hydrophilic proteins of approx. 45 kDa. Qualitative analysis of glycolipid composition showed that the T. cruzi strains and Dm28c clone and T. dionisii had four orcinol-positive spots, whereas in the other non-pathogenic trypanosomatids only three glycolipids were detected.

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Section: Discussionmentioning

confidence: 99%

Glycolipid and protein profiles in trypanosomatids

et al. 1994

Parasitol Res

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Use of glycoconjugates for trypanosomatid taxonomy

Branquinha

Meirelles

Lopes

et al. 1995

Current Microbiology

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Glycoconjugates from five trypanosomatid genera--Crithidia, Herpetomonas, Endotrypanum, Leishmania, and Trypanosoma--were extracted with Triton X-114 and analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis followed by periodic acid-Schiff staining. Most of the glycoconjugates were detected in the hydrophobic phase, indicating the presence of anchored glycoconjugates. All the trypanosomatids expressed a glycoconjugate with a low molecular weight (below 20 kDa) in this phase. In each species, however, a characteristic and specific pattern of glycoconjugates was also observed in both phases. In the hydrophobic phase: 14-29 kDa glycoconjugates in C. guilhermei; 24-70 kDa in C. fasciculata, C. luciliae, E. schaudinni, and T. cruzi Y and G strains; 45-66 kDa in C. oncopelti and H. samuelpessoai; above 36 kDa in T. dionisii; 20-24 kDa, 36-45 kDa, and 70 kDa in L. tarentolae and T. mega. In the hydrophilic phase, typical glycoproteins were observed in some trypanosomatids: 60 kDa in T. mega and T. cruzi Y strain; 70 kDa in H. samuelpessoai; 66 kDa in C. oncopelti; 20-70 kDa in C. luciliae. These findings suggest that Triton X-114-extracted glycoconjugates could be useful markers for trypanosomatid taxonomy.

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