Characterization of the infective properties of a new genetic group of Trypanosoma cruzi associated with bats

BAT, a representative strain of a new Trypanosoma cruzi genotype associated with bats, invaded host cells through lysosome exocytosis induced by the surface molecule gp82. [Display omitted] ► We characterized a representative strain from a new genetic group of Trypanosoma cruzi. ► This parasite stra...

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Veröffentlicht in:Acta tropica 2011-12, Vol.120 (3), p.231-237
Hauptverfasser: Maeda, Fernando Yukio, Alves, Renan Melatto, Cortez, Cristian, Lima, Fabio Mitsuo, Yoshida, Nobuko
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container_start_page 231
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creator Maeda, Fernando Yukio
Alves, Renan Melatto
Cortez, Cristian
Lima, Fabio Mitsuo
Yoshida, Nobuko
description BAT, a representative strain of a new Trypanosoma cruzi genotype associated with bats, invaded host cells through lysosome exocytosis induced by the surface molecule gp82. [Display omitted] ► We characterized a representative strain from a new genetic group of Trypanosoma cruzi. ► This parasite strain isolated from bat infected cultured human cells. ► We identified the parasite surface molecule implicated in host cell invasion. ► The parasite was poorly infective in mice. A new genotype of Trypanosoma cruzi, associated with bats from anthropic areas, was recently described. Here we characterized a T. cruzi strain from this new genetic group, which could be a potential source of infection to humans. Metacyclic trypomastigotes (MT) of this strain, herein designated BAT, were compared to MT of well characterized CL and G strains, as regards the surface profile and infectivity toward human epithelial HeLa cells. BAT strain MT expressed gp82, the surface molecule recognized by monoclonal antibody 3F6 and known to promote CL strain invasion by inducing lysosomal exocytosis, as well as mucin-like molecules, but lacked gp90, which functions as a negative regulator of invasion in G strain. A set of experiments indicated that BAT strain internalization is gp82-mediated, and requires the activation of host cell phosphatidylinositol 3-kinase, protein kinase C and the mammalian target of rapamycin. MT of BAT strain were able to migrate through a gastric mucin layer, a property associated with p82 and relevant for oral infection. Gp82 was found to be a highly conserved molecule. Analysis of the BAT strain gp82 domain, containing the cell binding- and gastric mucin-binding sites, showed 91 and 93% sequence identity with G and CL strains, respectively. Hela cell invasion by BAT strain MT was inhibited by purified mucin-like molecules, which were shown to affect lysosome exocytosis required for MT internalization. Although MT of BAT strain infected host cells in vitro, they were less effective than G or CL strains in infecting mice either orally or intraperitoneally.
doi_str_mv 10.1016/j.actatropica.2011.09.001
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Hela cell invasion by BAT strain MT was inhibited by purified mucin-like molecules, which were shown to affect lysosome exocytosis required for MT internalization. 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[Display omitted] ► We characterized a representative strain from a new genetic group of Trypanosoma cruzi. ► This parasite strain isolated from bat infected cultured human cells. ► We identified the parasite surface molecule implicated in host cell invasion. ► The parasite was poorly infective in mice. A new genotype of Trypanosoma cruzi, associated with bats from anthropic areas, was recently described. Here we characterized a T. cruzi strain from this new genetic group, which could be a potential source of infection to humans. Metacyclic trypomastigotes (MT) of this strain, herein designated BAT, were compared to MT of well characterized CL and G strains, as regards the surface profile and infectivity toward human epithelial HeLa cells. BAT strain MT expressed gp82, the surface molecule recognized by monoclonal antibody 3F6 and known to promote CL strain invasion by inducing lysosomal exocytosis, as well as mucin-like molecules, but lacked gp90, which functions as a negative regulator of invasion in G strain. A set of experiments indicated that BAT strain internalization is gp82-mediated, and requires the activation of host cell phosphatidylinositol 3-kinase, protein kinase C and the mammalian target of rapamycin. MT of BAT strain were able to migrate through a gastric mucin layer, a property associated with p82 and relevant for oral infection. Gp82 was found to be a highly conserved molecule. Analysis of the BAT strain gp82 domain, containing the cell binding- and gastric mucin-binding sites, showed 91 and 93% sequence identity with G and CL strains, respectively. Hela cell invasion by BAT strain MT was inhibited by purified mucin-like molecules, which were shown to affect lysosome exocytosis required for MT internalization. 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[Display omitted] ► We characterized a representative strain from a new genetic group of Trypanosoma cruzi. ► This parasite strain isolated from bat infected cultured human cells. ► We identified the parasite surface molecule implicated in host cell invasion. ► The parasite was poorly infective in mice. A new genotype of Trypanosoma cruzi, associated with bats from anthropic areas, was recently described. Here we characterized a T. cruzi strain from this new genetic group, which could be a potential source of infection to humans. Metacyclic trypomastigotes (MT) of this strain, herein designated BAT, were compared to MT of well characterized CL and G strains, as regards the surface profile and infectivity toward human epithelial HeLa cells. BAT strain MT expressed gp82, the surface molecule recognized by monoclonal antibody 3F6 and known to promote CL strain invasion by inducing lysosomal exocytosis, as well as mucin-like molecules, but lacked gp90, which functions as a negative regulator of invasion in G strain. A set of experiments indicated that BAT strain internalization is gp82-mediated, and requires the activation of host cell phosphatidylinositol 3-kinase, protein kinase C and the mammalian target of rapamycin. MT of BAT strain were able to migrate through a gastric mucin layer, a property associated with p82 and relevant for oral infection. Gp82 was found to be a highly conserved molecule. Analysis of the BAT strain gp82 domain, containing the cell binding- and gastric mucin-binding sites, showed 91 and 93% sequence identity with G and CL strains, respectively. Hela cell invasion by BAT strain MT was inhibited by purified mucin-like molecules, which were shown to affect lysosome exocytosis required for MT internalization. Although MT of BAT strain infected host cells in vitro, they were less effective than G or CL strains in infecting mice either orally or intraperitoneally.</abstract><cop>Oxford</cop><pub>Elsevier B.V</pub><pmid>21925137</pmid><doi>10.1016/j.actatropica.2011.09.001</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record>
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subjects Animals
Biological and medical sciences
Cell invasion, Bats
Chagas Disease - parasitology
Chagas Disease - veterinary
Chiroptera - parasitology
DNA, Protozoan - chemistry
DNA, Protozoan - genetics
Endocytosis
Epithelial Cells - parasitology
Female
Gene Expression Profiling
General aspects
HeLa Cells
Humans
Medical sciences
Membrane Proteins - biosynthesis
Membrane Proteins - genetics
Metacyclic forms
Mice
Mice, Inbred BALB C
Molecular Sequence Data
New genotype
Protozoan Proteins - biosynthesis
Protozoan Proteins - genetics
Sequence Analysis, DNA
Trypanosoma cruzi
Trypanosoma cruzi - classification
Trypanosoma cruzi - genetics
Trypanosoma cruzi - isolation & purification
title Characterization of the infective properties of a new genetic group of Trypanosoma cruzi associated with bats
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