Trypomastigotes in cultures of Blastocrithidia culicis (Novy, MacNeal &amp; Torrey, 1907) (Kinetoplastida: Trypanosomatidae)

Sousa, Maria Auxiliadora de

doi:10.1590/s0074-02761994000100018

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“…Blastocrithidia culicis is an insect trypanosomatid, found in the midgut of different culicidae species, which harbours an endosymbiotic bacterium in its cytoplasm, and presents the amastigote, promastigote and epimastigote forms (Wallace, 1966). Additionally, B. culicis was able to differentiate into trypomastigotes in vitro, which are similar to those observed during T. cruzi metacyclogenesis (Sousa, 1994), a fact that emphasizes the importance of biochemical studies in this species.…”

Section: Introductionmentioning

confidence: 76%

Proteolytic expression inBlastocrithidia culicis: influence of the endosymbiont and similarities with virulence factors of pathogenic trypanosomatids

et al. 2004

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Blastocrithidia culicis is an insect trypanosomatid that presents bacterial endosymbionts. The cell-associated and secreted proteinases of the endosymbiont-bearing and aposymbiotic strains were compared through the incorporation of proteinaceous substrates into sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Few qualitative changes could be detected in the proteolytic zymograms in the 2 strains studied when gelatin, casein, haemoglobin or bovine serum albumin (BSA) were tested. However, the level of proteolytic activities was significantly higher in the aposymbiotic strain. Some of the B. culicis proteins reacted in Western blots with antibodies raised against gp63, a zinc-metalloproteinase, and cruzipain, a cysteinyl-proteinase, which are virulence factors of the human pathogenic trypanosomatids, Leishmania spp. and Trypanosoma cruzi, respectively. The anti-cross-reacting determinant (CRD) antibody recognized 2 polypeptides (50 and 58 kDa) in the spent culture media and in the supernatant from glycosylphosphatidylinositol-phospholipase C (GPI-PLC)-treated cells, suggesting that these proteins are GPI-anchored to the plasma membrane. In addition, the anti-gp63 reacted with the 50 kDa protein. The identification of protein homologues in trypanosomatids with distinct life-cycles may help to determine the importance of proteinases in trypanosomatids.

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Section: Introductionmentioning

confidence: 76%

Proteolytic expression inBlastocrithidia culicis: influence of the endosymbiont and similarities with virulence factors of pathogenic trypanosomatids

et al. 2004

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Cell-Associated and Extracellular Proteinases in Blastocrithidia culicis : Influence of Growth Conditions

Santos

Abreu

Batista

et al. 2001

Current Microbiology

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The proteinase profile of Blastocrithidia culicis was analyzed, as well as how different growth conditions influenced its expression by gelatin-SDS-PAGE and the use of specific proteinase inhibitors. Multiple cell-associated proteinases with molecular masses corresponding to 33, 55, 60 kDa (cysteine proteinases) and 77, 80, 90, and 108 kDa (metalloproteinases) were detected using these methods. All the metalloproteinases identified were partitioned into the detergent phase after Triton X-114 extract, suggesting that they are membrane-bound, while all cysteine proteinases were partitioned into the aqueous phase. The proteolytic zymograms were similar when three different media were used for variable times of incubation. However, few quantitative and qualitative changes were observed. The secreted proteinase profile showed an heterogeneous pattern of enzymatic activities whose expression was dependent on time of growth and medium composition. However, the extracellular proteinase activities were abolished by 1,10-phenanthroline, suggesting that all of them are zinc-metalloproteinases.

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Hidden life cycle stages of the trypanosomatid Blastocrithidia triatomae Cerisola et al. 1971 (Protista: Excavata: Kinetoplastea) unveiled by a new cultivation method

JÚNIOR,

PAIVA,

PACHECO

et al. 2024

Zootaxa

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Blastocrithidia triatomae is a monoxenic trypanosomatid parasite of triatomines, sharing the same insect vectors with Trypanosoma cruzi Chagas, 1909 and T. rangeli Tejera, 1920. It is known to cause a complex syndrome in insects which induces severe metabolic disorders and increasing in mortality rates. In the present study, we established an efficient serial axenic cultivation method for B. triatomae using a new medium, herein called MBT, which revealed previously unknown morphotypes, named microepimastigotes and sinemastigotes, not found in specific cell linage cultures. The results improve the knowledge on the life cycle of genus Blastocrithidia Laird 1959, its distinction from other trypanosomatids, such as T. cruzi and T. rangeli, and settle new ground for thorough exploration of morphological features and its application for trypanosomatid systematics.

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Trypomastigotes in cultures of Blastocrithidia culicis (Novy, MacNeal & Torrey, 1907) (Kinetoplastida: Trypanosomatidae)

Cited by 3 publications

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Proteolytic expression inBlastocrithidia culicis: influence of the endosymbiont and similarities with virulence factors of pathogenic trypanosomatids

Proteolytic expression inBlastocrithidia culicis: influence of the endosymbiont and similarities with virulence factors of pathogenic trypanosomatids

Cell-Associated and Extracellular Proteinases in Blastocrithidia culicis : Influence of Growth Conditions

Hidden life cycle stages of the trypanosomatid Blastocrithidia triatomae Cerisola et al. 1971 (Protista: Excavata: Kinetoplastea) unveiled by a new cultivation method

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