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Catherine Texier - One of the best experts on this subject based on the ideXlab platform.
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enp1 and enp2 two proteins associated with the encephalitozoon cuniculi endoSpore the chitin rich inner layer of the Microsporidian Spore wall
International Journal for Parasitology, 2006Co-Authors: Isabelle Peuvelfanget, Damien Brosson, Lauriane Kuhn, Christian P. Vivarès, Catherine Texier, Valerie Polonais, Pierre Peyret, Frederic DelbacAbstract:Abstract Microsporidia are obligate intracellular parasites forming environmentally resistant Spores that harbour a rigid cell wall. This wall comprises an outer layer or exoSpore and a chitin-rich inner layer or endoSpore. So far, only a chitin deacetylase-like protein has been shown to localize to the Encephalitozoon cuniculi endoSpore and either one or two proteins have been clearly assigned to the exoSpore in two Encephalitozoon species: SWP1 in E. cuniculi, SWP1 and SWP2 in Encephalitozoon intestinalis. Here, we report the identification of two new Spore wall proteins in E. cuniculi, EnP1 and EnP2, the genes of which are both located on chromosome I (ECU01_0820 and ECU01_1270, respectively) and have no known homologue. Detected by immunoscreening of an E. cuniculi cDNA library, enp1 is characterized by small-sized 5′ and 3′ untranslated regions and is highly expressed throughout the whole intracellular cycle. The encoded basic 40 kDa antigen displays a high proportion of cysteine residues, arguing for a significant role of disulfide bridges in Spore wall assembly. EnP2 is a 22 kDa serine-rich protein that is predicted to be O-glycosylated and glycosylated phosphatidyl inositol-anchored. Although having been identified by mass spectrometry of a dithiothreitol-soluble fraction, this protein contains only two cysteine residues. Mouse polyclonal antibodies were raised against EnP1 and EnP2 recombinant proteins produced in Escherichia coli Our immunolocalisation data indicate that EnP1 and EnP2 are targeted to the cell surface as early as the onset of sporogony and are finally associated with the chitin-rich layer of the wall in mature Spores.
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The putative chitin deacetylase of Encephalitozoon cuniculi: A surface protein implicated in Microsporidian Spore‐wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.
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the putative chitin deacetylase of encephalitozoon cuniculi a surface protein implicated in Microsporidian Spore wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.
Earl Weidner - One of the best experts on this subject based on the ideXlab platform.
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Differentiation of Microsporidian Spore-tails in Inodosporus spraguei gen. et sp. n.
Parasitology Research, 2018Co-Authors: Robin M. Overstreet, Earl WeidnerAbstract:The new genus Inodosporus was erected to accept I. spraguei, a new species having eight sporoblasts per pansporoblast with each subsequent Spore possessing three or four basal Spore-tails and one branched apical one. It is primarily by the apical tail that the species is separated from the only other recognized species, I. octospora (Henneguy, 1892) comb. n., formerly Thelohania octospora.
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The Microsporidian Spore Invasion Tube. III. Tube Extrusion and Assembly
2013Co-Authors: Earl WeidnerAbstract:ABSTRACT The polar filaments within Microsporidian Spores discharge as tubes with subsecond velocity. Populations of discharging tubes of Glugea hertwigi Spores pulse-labeled with latex particles for 1-3 s were consistently devoid of label at the distal ends; discharging tubes were completely labeled after 30- to 60-s exposure to latex. This experiment indicates that discharge tubes grow at the tip. Completely assembled discharge tubes consisted of single, empty cylinders; however, incompletely discharged tubes had a cylinder-within-a-cylinder profile at the distal ends. This observation indicates that the discharge tube material emerges at the distal end by an eversion process. Finally, studies with cinematic Nomarski interference optics of Spore tubes extruding across a water-air interphase indicate that all the material emerging from the growing tip of the tube is incorporated into the wall of the discharge tube. Evidence indicates that the polar filament of undischarged Spores is a homogeneous coil of polar tube protein equivalent to the polar tube protein in discharged tubes. Microsporidia have the capacity to inoculate a cell from a Spore stage into a host cell by means of an invasion tube (1-3, 8). Microsporidian parasites are intracellular eukaryotes wit
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Microsporidian Spore/Sporoplasm Dynactin in Spraguea
The Biological Bulletin, 2001Co-Authors: Earl WeidnerAbstract:440. 7. Brown, A., and R. J. Lasek. 1990. Pp. 235–302 in Squid as Experimental Animals. D. L. Gilbert, W. J. Adelman, Jr., and J. M. Arnold, eds., Plenum Press, New York. 8. Grant, P., D. Tseng, R. M. Gould, H. Gainer, and H. C. Pant. 1995. J. Comp. Neurol. 356: 311–326. 9. Tsai, M.-Y., G. Morfini, G. Szebenyi, and S. T. Brady. 2000. Mol. Biol. Cell 11: 2161–2173. 10. Hollenbeck, P. J. 1989. J. Cell Biol. 108: 2335–2342.
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Microsporidian Spore sporoplasm dynactin in spraguea
The Biological Bulletin, 2001Co-Authors: Earl WeidnerAbstract:440. 7. Brown, A., and R. J. Lasek. 1990. Pp. 235–302 in Squid as Experimental Animals. D. L. Gilbert, W. J. Adelman, Jr., and J. M. Arnold, eds., Plenum Press, New York. 8. Grant, P., D. Tseng, R. M. Gould, H. Gainer, and H. C. Pant. 1995. J. Comp. Neurol. 356: 311–326. 9. Tsai, M.-Y., G. Morfini, G. Szebenyi, and S. T. Brady. 2000. Mol. Biol. Cell 11: 2161–2173. 10. Hollenbeck, P. J. 1989. J. Cell Biol. 108: 2335–2342.
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Protein-Membrane Interaction Is Essential to Normal Assembly of the Microsporidian Spore Invasion Tube.
The Biological Bulletin, 1995Co-Authors: Earl Weidner, Sandra K. Halonen, S. B. Manale, J. W. LynnAbstract:Changes in the protein-membrane interaction during assembly of the Microsporidian Spore invasion tubes were followed by electron microscopy, by video imaging with differential interference contrast (DIC), and by the fluorescent probes 4',6-diamidino-2-phenylindole (DAPI) and 9-diethylamino-5H-benzo{alpha}phenoxazine-5-one (Nile red). Microsporidian Spore invasion tubes form by the eversion of polar filament protein (PFP) and presumptive extrusion apparatus (EAP) membrane. Both of these components are essential for formation of the invasion tube. The results indicate that the behavior of the EAP membrane is greatly affected by the position and chemical state of the PFP at the eversion area that constitutes the advancing tube terminal assembly site (TAS). Visual evidence indicates that the EAP membrane is the vehicle for PFP and that this membrane also provides the envelope that surrounds the sporoplasm after its passage through the invasion tube.
Damien Brosson - One of the best experts on this subject based on the ideXlab platform.
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enp1 and enp2 two proteins associated with the encephalitozoon cuniculi endoSpore the chitin rich inner layer of the Microsporidian Spore wall
International Journal for Parasitology, 2006Co-Authors: Isabelle Peuvelfanget, Damien Brosson, Lauriane Kuhn, Christian P. Vivarès, Catherine Texier, Valerie Polonais, Pierre Peyret, Frederic DelbacAbstract:Abstract Microsporidia are obligate intracellular parasites forming environmentally resistant Spores that harbour a rigid cell wall. This wall comprises an outer layer or exoSpore and a chitin-rich inner layer or endoSpore. So far, only a chitin deacetylase-like protein has been shown to localize to the Encephalitozoon cuniculi endoSpore and either one or two proteins have been clearly assigned to the exoSpore in two Encephalitozoon species: SWP1 in E. cuniculi, SWP1 and SWP2 in Encephalitozoon intestinalis. Here, we report the identification of two new Spore wall proteins in E. cuniculi, EnP1 and EnP2, the genes of which are both located on chromosome I (ECU01_0820 and ECU01_1270, respectively) and have no known homologue. Detected by immunoscreening of an E. cuniculi cDNA library, enp1 is characterized by small-sized 5′ and 3′ untranslated regions and is highly expressed throughout the whole intracellular cycle. The encoded basic 40 kDa antigen displays a high proportion of cysteine residues, arguing for a significant role of disulfide bridges in Spore wall assembly. EnP2 is a 22 kDa serine-rich protein that is predicted to be O-glycosylated and glycosylated phosphatidyl inositol-anchored. Although having been identified by mass spectrometry of a dithiothreitol-soluble fraction, this protein contains only two cysteine residues. Mouse polyclonal antibodies were raised against EnP1 and EnP2 recombinant proteins produced in Escherichia coli Our immunolocalisation data indicate that EnP1 and EnP2 are targeted to the cell surface as early as the onset of sporogony and are finally associated with the chitin-rich layer of the wall in mature Spores.
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The putative chitin deacetylase of Encephalitozoon cuniculi: A surface protein implicated in Microsporidian Spore‐wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.
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the putative chitin deacetylase of encephalitozoon cuniculi a surface protein implicated in Microsporidian Spore wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.
Christian P. Vivarès - One of the best experts on this subject based on the ideXlab platform.
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enp1 and enp2 two proteins associated with the encephalitozoon cuniculi endoSpore the chitin rich inner layer of the Microsporidian Spore wall
International Journal for Parasitology, 2006Co-Authors: Isabelle Peuvelfanget, Damien Brosson, Lauriane Kuhn, Christian P. Vivarès, Catherine Texier, Valerie Polonais, Pierre Peyret, Frederic DelbacAbstract:Abstract Microsporidia are obligate intracellular parasites forming environmentally resistant Spores that harbour a rigid cell wall. This wall comprises an outer layer or exoSpore and a chitin-rich inner layer or endoSpore. So far, only a chitin deacetylase-like protein has been shown to localize to the Encephalitozoon cuniculi endoSpore and either one or two proteins have been clearly assigned to the exoSpore in two Encephalitozoon species: SWP1 in E. cuniculi, SWP1 and SWP2 in Encephalitozoon intestinalis. Here, we report the identification of two new Spore wall proteins in E. cuniculi, EnP1 and EnP2, the genes of which are both located on chromosome I (ECU01_0820 and ECU01_1270, respectively) and have no known homologue. Detected by immunoscreening of an E. cuniculi cDNA library, enp1 is characterized by small-sized 5′ and 3′ untranslated regions and is highly expressed throughout the whole intracellular cycle. The encoded basic 40 kDa antigen displays a high proportion of cysteine residues, arguing for a significant role of disulfide bridges in Spore wall assembly. EnP2 is a 22 kDa serine-rich protein that is predicted to be O-glycosylated and glycosylated phosphatidyl inositol-anchored. Although having been identified by mass spectrometry of a dithiothreitol-soluble fraction, this protein contains only two cysteine residues. Mouse polyclonal antibodies were raised against EnP1 and EnP2 recombinant proteins produced in Escherichia coli Our immunolocalisation data indicate that EnP1 and EnP2 are targeted to the cell surface as early as the onset of sporogony and are finally associated with the chitin-rich layer of the wall in mature Spores.
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The putative chitin deacetylase of Encephalitozoon cuniculi: A surface protein implicated in Microsporidian Spore‐wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.
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the putative chitin deacetylase of encephalitozoon cuniculi a surface protein implicated in Microsporidian Spore wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.
Lauriane Kuhn - One of the best experts on this subject based on the ideXlab platform.
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enp1 and enp2 two proteins associated with the encephalitozoon cuniculi endoSpore the chitin rich inner layer of the Microsporidian Spore wall
International Journal for Parasitology, 2006Co-Authors: Isabelle Peuvelfanget, Damien Brosson, Lauriane Kuhn, Christian P. Vivarès, Catherine Texier, Valerie Polonais, Pierre Peyret, Frederic DelbacAbstract:Abstract Microsporidia are obligate intracellular parasites forming environmentally resistant Spores that harbour a rigid cell wall. This wall comprises an outer layer or exoSpore and a chitin-rich inner layer or endoSpore. So far, only a chitin deacetylase-like protein has been shown to localize to the Encephalitozoon cuniculi endoSpore and either one or two proteins have been clearly assigned to the exoSpore in two Encephalitozoon species: SWP1 in E. cuniculi, SWP1 and SWP2 in Encephalitozoon intestinalis. Here, we report the identification of two new Spore wall proteins in E. cuniculi, EnP1 and EnP2, the genes of which are both located on chromosome I (ECU01_0820 and ECU01_1270, respectively) and have no known homologue. Detected by immunoscreening of an E. cuniculi cDNA library, enp1 is characterized by small-sized 5′ and 3′ untranslated regions and is highly expressed throughout the whole intracellular cycle. The encoded basic 40 kDa antigen displays a high proportion of cysteine residues, arguing for a significant role of disulfide bridges in Spore wall assembly. EnP2 is a 22 kDa serine-rich protein that is predicted to be O-glycosylated and glycosylated phosphatidyl inositol-anchored. Although having been identified by mass spectrometry of a dithiothreitol-soluble fraction, this protein contains only two cysteine residues. Mouse polyclonal antibodies were raised against EnP1 and EnP2 recombinant proteins produced in Escherichia coli Our immunolocalisation data indicate that EnP1 and EnP2 are targeted to the cell surface as early as the onset of sporogony and are finally associated with the chitin-rich layer of the wall in mature Spores.
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The putative chitin deacetylase of Encephalitozoon cuniculi: A surface protein implicated in Microsporidian Spore‐wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.
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the putative chitin deacetylase of encephalitozoon cuniculi a surface protein implicated in Microsporidian Spore wall formation
Fems Microbiology Letters, 2005Co-Authors: Damien Brosson, Lauriane Kuhn, Gérard Prensier, Christian P. Vivarès, Catherine TexierAbstract:Microsporidia are fungal-like unicellular eukaryotes which develop as obligate intracellular parasites. They differentiate into resistant Spores that are protected by a thick cell wall composed of glycoproteins and chitin. Despite an extensive description of the fibrillar structure of this wall, very little is known about its protein components and deposit mechanisms. In this study on the human pathogen Encephalitozoon cuniculi, we identify by mass spectrometry the target of polyclonal antibodies previously raised against a 33-kDa protein located at the outer face of the parasite plasma membrane. This 254-amino acid protein is encoded by the ECU11_0510 open reading frame and presents two isoforms of 33 and 55 kDa. Sequence analysis supports an assignment to the polysaccharide deacetylase family with a suspected chitin deacetylase activity (EcCDA). As demonstrated by TEM studies, EcCDA is present at the plasma membrane of the early stages of E. cuniculi life-cycle. At the sporoblast stage, the enzyme accumulates especially in paramural bodies which are convolutions of the plasma membrane opened to the wall. The identification of an EcCDA homologue in the insect parasite Antonospora locustae (ex Nosema locustae) suggests a widespread distribution of this enzyme among Microsporidia. This characterization of a new Microsporidian surface protein creates new perspectives to understand Spore wall formation and Spore resistance.