2006
DOI: 10.1590/s0001-37652006000400006
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Abstract: Plant and insect trypanosomatids constitute the " lower trypanosomatids", which have been used routinely as laboratory models for biochemical and molecular studies because they are easily cultured under axenic conditions, and they contain homologues of virulence factors from the classic human trypanosomatid pathogens. Among the molecular factors that contribute to Leishmania spp. virulence and pathogenesis, the major surface protease, alternatively called MSP, PSP, leishmanolysin, EC 3.4.24.36 and gp63, is the… Show more

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Cited by 56 publications
(66 citation statements)
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“…Vesicles containing both membrane-bound and free gp63 fuse with the flagellar pocket membrane and thereafter the free gp63 is released extracellularly [30], while the membrane-bound form is located throughout the external cell membrane and a proportion of this is released directly via autoproteolysis [19], in a similar mechanism to that observed in Leishmania [160,161]. Both cellular and released gp63-like molecules had similar biochemical features, including optimum pH around 5.0-6.5 (the prevailing pH range of the insect gut and the pH of phagolysosome), susceptibility to metallo-type peptidase inhibitors mainly 1,10-phenanthroline, molecular mass around 50-70 kDa, immunological reactivity against antigp63 antibodies, best temperature at 37ºC (mammalian temperature) instead of 26ºC (invertebrate temperature) and broad hydrolytic capability (degrading gelatin, hemoglobin, casein, albumin, mucin, immunoglobulin and insect proteinaceous components), corroborating the hypothesis of conservation of an ancient and functionally relevant molecule shared by both heteroxenous and monoxenous trypanosomatids [15].…”
Section: Metallopeptidases: Gp63-likesupporting
confidence: 64%
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“…Vesicles containing both membrane-bound and free gp63 fuse with the flagellar pocket membrane and thereafter the free gp63 is released extracellularly [30], while the membrane-bound form is located throughout the external cell membrane and a proportion of this is released directly via autoproteolysis [19], in a similar mechanism to that observed in Leishmania [160,161]. Both cellular and released gp63-like molecules had similar biochemical features, including optimum pH around 5.0-6.5 (the prevailing pH range of the insect gut and the pH of phagolysosome), susceptibility to metallo-type peptidase inhibitors mainly 1,10-phenanthroline, molecular mass around 50-70 kDa, immunological reactivity against antigp63 antibodies, best temperature at 37ºC (mammalian temperature) instead of 26ºC (invertebrate temperature) and broad hydrolytic capability (degrading gelatin, hemoglobin, casein, albumin, mucin, immunoglobulin and insect proteinaceous components), corroborating the hypothesis of conservation of an ancient and functionally relevant molecule shared by both heteroxenous and monoxenous trypanosomatids [15].…”
Section: Metallopeptidases: Gp63-likesupporting
confidence: 64%
“…In addition, because of their unusual structural features, developing a new generation of chemotherapeutic agents for parasitic diseases, such as Chagas' disease and leishmaniasis, is also a critical research priority. Furthermore, the lower trypanosomatids share similar molecules from classical trypanosomatid pathogens, including virulence factors like peptidases [15,17]. These observations indicate that the life cycle of lower trypanosomatids has been underestimated and that homologous to virulence attributes from pathogens should fulfill a more diverse role for these trypanosomatids than previously thought and confirm their importance as a model for biochemical and molecular studies among the trypanosomatids.…”
Section: Perspectivessupporting
confidence: 51%
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“…I am a peer reviewer for international scientific journals, as well as career and research grant committees. In addition, I have accepted invitations to write reviews and book chapters on the themes: (1) relevance of proteolytic enzymes produced by microorganisms; and (2) antimicrobial properties of protease inhibitors [1][2][3][4][5][6][7][8][9][10][11] . Over the last years, my group has focused on the identification, biochemical characterization and discovery of biological functions of proteases produced by microorganisms, with emphasis in trypanosomatids and fungi ( Figure 3).…”
Section: Introduction and Educational Experiencementioning
confidence: 99%