A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence

ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries. Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Nathan M. Chasen [verfasserIn] Beejan Asady [verfasserIn] Leandro Lemgruber [verfasserIn] Rossiane C. Vommaro [verfasserIn] Jessica C. Kissinger [verfasserIn] Isabelle Coppens [verfasserIn] Silvia N. J. Moreno [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2017

Schlagwörter:	carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry

Übergeordnetes Werk:	In: mSphere - American Society for Microbiology, 2016, 2(2017), 3
Übergeordnetes Werk:	volume:2 ; year:2017 ; number:3

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1128/mSphere.00027-17

Katalog-ID:	DOAJ063323850

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245	1	2	\|a A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence
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520			\|a ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries.
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allfields	10.1128/mSphere.00027-17 doi (DE-627)DOAJ063323850 (DE-599)DOAJ60ddfb8fd73a43078878e276965dd038 DE-627 ger DE-627 rakwb eng QR1-502 Nathan M. Chasen verfasserin aut A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries. carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry Microbiology Beejan Asady verfasserin aut Leandro Lemgruber verfasserin aut Rossiane C. Vommaro verfasserin aut Jessica C. Kissinger verfasserin aut Isabelle Coppens verfasserin aut Silvia N. J. Moreno verfasserin aut In mSphere American Society for Microbiology, 2016 2(2017), 3 (DE-627)845748807 (DE-600)2844248-9 23795042 nnns volume:2 year:2017 number:3 https://doi.org/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/article/60ddfb8fd73a43078878e276965dd038 kostenfrei https://journals.asm.org/doi/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/toc/2379-5042 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2017 3
spelling	10.1128/mSphere.00027-17 doi (DE-627)DOAJ063323850 (DE-599)DOAJ60ddfb8fd73a43078878e276965dd038 DE-627 ger DE-627 rakwb eng QR1-502 Nathan M. Chasen verfasserin aut A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries. carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry Microbiology Beejan Asady verfasserin aut Leandro Lemgruber verfasserin aut Rossiane C. Vommaro verfasserin aut Jessica C. Kissinger verfasserin aut Isabelle Coppens verfasserin aut Silvia N. J. Moreno verfasserin aut In mSphere American Society for Microbiology, 2016 2(2017), 3 (DE-627)845748807 (DE-600)2844248-9 23795042 nnns volume:2 year:2017 number:3 https://doi.org/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/article/60ddfb8fd73a43078878e276965dd038 kostenfrei https://journals.asm.org/doi/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/toc/2379-5042 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2017 3
allfields_unstemmed	10.1128/mSphere.00027-17 doi (DE-627)DOAJ063323850 (DE-599)DOAJ60ddfb8fd73a43078878e276965dd038 DE-627 ger DE-627 rakwb eng QR1-502 Nathan M. Chasen verfasserin aut A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries. carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry Microbiology Beejan Asady verfasserin aut Leandro Lemgruber verfasserin aut Rossiane C. Vommaro verfasserin aut Jessica C. Kissinger verfasserin aut Isabelle Coppens verfasserin aut Silvia N. J. Moreno verfasserin aut In mSphere American Society for Microbiology, 2016 2(2017), 3 (DE-627)845748807 (DE-600)2844248-9 23795042 nnns volume:2 year:2017 number:3 https://doi.org/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/article/60ddfb8fd73a43078878e276965dd038 kostenfrei https://journals.asm.org/doi/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/toc/2379-5042 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2017 3
allfieldsGer	10.1128/mSphere.00027-17 doi (DE-627)DOAJ063323850 (DE-599)DOAJ60ddfb8fd73a43078878e276965dd038 DE-627 ger DE-627 rakwb eng QR1-502 Nathan M. Chasen verfasserin aut A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries. carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry Microbiology Beejan Asady verfasserin aut Leandro Lemgruber verfasserin aut Rossiane C. Vommaro verfasserin aut Jessica C. Kissinger verfasserin aut Isabelle Coppens verfasserin aut Silvia N. J. Moreno verfasserin aut In mSphere American Society for Microbiology, 2016 2(2017), 3 (DE-627)845748807 (DE-600)2844248-9 23795042 nnns volume:2 year:2017 number:3 https://doi.org/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/article/60ddfb8fd73a43078878e276965dd038 kostenfrei https://journals.asm.org/doi/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/toc/2379-5042 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2017 3
allfieldsSound	10.1128/mSphere.00027-17 doi (DE-627)DOAJ063323850 (DE-599)DOAJ60ddfb8fd73a43078878e276965dd038 DE-627 ger DE-627 rakwb eng QR1-502 Nathan M. Chasen verfasserin aut A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence 2017 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries. carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry Microbiology Beejan Asady verfasserin aut Leandro Lemgruber verfasserin aut Rossiane C. Vommaro verfasserin aut Jessica C. Kissinger verfasserin aut Isabelle Coppens verfasserin aut Silvia N. J. Moreno verfasserin aut In mSphere American Society for Microbiology, 2016 2(2017), 3 (DE-627)845748807 (DE-600)2844248-9 23795042 nnns volume:2 year:2017 number:3 https://doi.org/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/article/60ddfb8fd73a43078878e276965dd038 kostenfrei https://journals.asm.org/doi/10.1128/mSphere.00027-17 kostenfrei https://doaj.org/toc/2379-5042 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 2 2017 3
language	English
source	In mSphere 2(2017), 3 volume:2 year:2017 number:3
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topic_facet	carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry Microbiology
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authorswithroles_txt_mv	Nathan M. Chasen @@aut@@ Beejan Asady @@aut@@ Leandro Lemgruber @@aut@@ Rossiane C. Vommaro @@aut@@ Jessica C. Kissinger @@aut@@ Isabelle Coppens @@aut@@ Silvia N. J. Moreno @@aut@@
publishDateDaySort_date	2017-01-01T00:00:00Z
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topic_title	QR1-502 A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence carbonic anhydrase infectivity Toxoplasma gondii glycosylphosphatidylinositols organelle structure rhoptry
topic	misc QR1-502 misc carbonic anhydrase misc infectivity misc Toxoplasma gondii misc glycosylphosphatidylinositols misc organelle structure misc rhoptry misc Microbiology
topic_unstemmed	misc QR1-502 misc carbonic anhydrase misc infectivity misc Toxoplasma gondii misc glycosylphosphatidylinositols misc organelle structure misc rhoptry misc Microbiology
topic_browse	misc QR1-502 misc carbonic anhydrase misc infectivity misc Toxoplasma gondii misc glycosylphosphatidylinositols misc organelle structure misc rhoptry misc Microbiology
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title	A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence
ctrlnum	(DE-627)DOAJ063323850 (DE-599)DOAJ60ddfb8fd73a43078878e276965dd038
title_full	A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence
author_sort	Nathan M. Chasen
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author_browse	Nathan M. Chasen Beejan Asady Leandro Lemgruber Rossiane C. Vommaro Jessica C. Kissinger Isabelle Coppens Silvia N. J. Moreno
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author-letter	Nathan M. Chasen
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title_sort	glycosylphosphatidylinositol-anchored carbonic anhydrase-related protein of <named-content content-type="genus-species"<toxoplasma gondii</named-content< is important for rhoptry biogenesis and virulence
callnumber	QR1-502
title_auth	A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence
abstract	ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries.
abstractGer	ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries.
abstract_unstemmed	ABSTRACT Carbonic anhydrase-related proteins (CARPs) have previously been described as catalytically inactive proteins closely related to α-carbonic anhydrases (α-CAs). These CARPs are found in animals (both vertebrates and invertebrates) and viruses as either independent proteins or domains of other proteins. We report here the identification of a new CARP (TgCA_RP) in the unicellular organism Toxoplasma gondii that is related to the recently described η-class CA found in Plasmodium falciparum. TgCA_RP is posttranslationally modified at its C terminus with a glycosylphosphatidylinositol anchor that is important for its localization in intracellular tachyzoites. The protein localizes throughout the rhoptry bulbs of mature tachyzoites and to the outer membrane of nascent rhoptries in dividing tachyzoites, as demonstrated by immunofluorescence and immunoelectron microscopy using specific antibodies. T. gondii mutant tachyzoites lacking TgCA_RP display a growth and invasion phenotype in vitro and have atypical rhoptry morphology. The mutants also exhibit reduced virulence in a mouse model. Our results show that TgCA_RP plays an important role in the biogenesis of rhoptries. IMPORTANCE Toxoplasma gondii is an intracellular pathogen that infects humans and animals. The pathogenesis of T. gondii is linked to its lytic cycle, which starts when tachyzoites invade host cells and secrete proteins from specialized organelles. Once inside the host cell, the parasite creates a parasitophorous vacuole (PV) where it divides. Rhoptries are specialized secretory organelles that contain proteins, many of which are secreted during invasion. These proteins have important roles not only during the initial interaction between parasite and host but also in the formation of the PV and in the modification of the host cell. We report here the identification of a new T. gondii carbonic anhydrase-related protein (TgCA_RP), which localizes to rhoptries of mature tachyzoites. TgCA_RP is important for the morphology of rhoptries and for invasion and growth of parasites. TgCA_RP is also critical for parasite virulence. We propose that TgCA_RP plays a role in the biogenesis of rhoptries.
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title_short	A Glycosylphosphatidylinositol-Anchored Carbonic Anhydrase-Related Protein of <named-content content-type="genus-species"<Toxoplasma gondii</named-content< Is Important for Rhoptry Biogenesis and Virulence
url	https://doi.org/10.1128/mSphere.00027-17 https://doaj.org/article/60ddfb8fd73a43078878e276965dd038 https://journals.asm.org/doi/10.1128/mSphere.00027-17 https://doaj.org/toc/2379-5042
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author2	Beejan Asady Leandro Lemgruber Rossiane C. Vommaro Jessica C. Kissinger Isabelle Coppens Silvia N. J. Moreno
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up_date	2024-07-03T17:04:05.052Z
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