Molecular structure of a Toxoplasma gondii dense granule antigen (GRA 5) associated with the parasitophorous vacuole membrane

Lecordier, Laurence; Mercier, Corinne; Torpier, Gérard; Tourvieille, B.; Darcy, F.; Liu, Jin Li; Mäes, Pierrette; Tartar, André; Càpron, André; Cesbron-Delauw, M.-F.

doi:10.1016/0166-6851(93)90015-p

Cited by 91 publications

(40 citation statements)

References 28 publications

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“…A second cDNA library of RH T. gondii tachyzoites constructed in lZAP w II, provided by L. Lecordier (Lecordier et al, 1993), was screened by hybridization with a digoxigenin-labelled 401 probe. The probe was prepared by random priming of the 401 insert (Boehringer Mannheim kit).…”

Section: Molecular Cloning and Sequence Analysis Of Mic3mentioning

confidence: 99%

The microneme protein MIC3 of Toxoplasma gondii is a secretory adhesin that binds to both the surface of the host cells and the surface of the parasite

Lebrun²,

et al. 2000

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SummaryAssay of the adhesion of cultured cells on Toxoplasma gondii tachyzoite protein Western blots identified a major adhesive protein, that migrated at 90 kDa in non-reducing gels. This band comigrated with the previously described microneme protein MIC3. Cellular binding on Western blots was abolished by MIC3-specific monoclonal and polyclonal antibodies. The MIC3 protein affinity purified from tachyzoite lysates bound to the surface of putative host cells. In addition, T. gondii tachyzoites also bound to immobilized MIC3. Immunofluorescence analysis of T. gondii tachyzoite invasion showed that MIC3 was exocytosed and relocalized to the surface of the parasite during invasion. The cDNA encoding MIC3 and the corresponding gene have been cloned, allowing the determination of the complete coding sequence. The MIC3 sequence has been confirmed by affinity purification of the native protein and N-terminal sequencing. The deduced protein sequence contains five partially overlapping EGF-like domains and a chitin binding-like domain, which can be involved in protein±protein or protein± carbohydrate interactions. Taken together, these results suggest that MIC3 is a new microneme adhesin of T. gondii.

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Section: Molecular Cloning and Sequence Analysis Of Mic3mentioning

confidence: 99%

The microneme protein MIC3 of Toxoplasma gondii is a secretory adhesin that binds to both the surface of the host cells and the surface of the parasite

Lebrun²,

et al. 2000

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“…GRA5, the P21 antigen of T. gondii, has been described as a dense granule component, secreted in the PV during host cell invasion [54]. The gene encoding GRA 5 is 834 bp long and does not contain any intron and the deduced amino acid sequence of an open reading frame encodes 133 amino acids of which a N-terminal hydrophobic region possesses the characteristics of a signal peptide of 25 amino acids and a second hydrophobic domain bordered by 2 hydrophilic regions strongly suggests a transmembrane region.…”

Section: Gra5mentioning

confidence: 99%

GRA Proteins of Toxoplasma gondii: Maintenance of Host-Parasite Interactions across the Parasitophorous Vacuolar Membrane

Nam

2009

Korean J Parasitol

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Abstract:The dense granule of Toxoplasma gondii is a secretory vesicular organelle of which the proteins participate in the modification of the parasitophorous vacuole (PV) and PV membrane for the maintenance of intracellular parasitism in almost all nucleated host cells. In this review, the archives on the research of GRA proteins are reviewed on the foci of finding GRA proteins, characterizing molecular aspects, usefulness in diagnostic antigen, and vaccine trials in addition to some functions in host-parasite interactions.

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“…TgPI-1 Remains Soluble after Secretion into the PV-After secretion into the PV, DG proteins can be targeted to the PV membrane (29,30) or the intravacuolar network of tubular membranes within the PV (25) or remain soluble (31). The solubility characteristics of a DG protein are important for predicting whether the protein will remain confined to the host cell after parasite egress or whether it will be released to…”

Section: Tgpi-1 Belongs To the Kazal Family Of Protease Inhibitors-mentioning

confidence: 99%

Functional Analysis of Toxoplasma gondii Protease Inhibitor 1

Morris¹,

Coppin²,

Tomavo³

et al. 2002

Journal of Biological Chemistry

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We have characterized a Kazal family serine protease inhibitor, Toxoplasma gondii protease inhibitor 1 (TgPI-1), in the obligate intracellular parasite Toxoplasma gondii. TgPI-1 contains four inhibitor domains predicted to inhibit trypsin, chymotrypsin, and elastase. Antibodies against recombinant TgPI-1 detect two polypeptides, of 43 and 41 kDa, designated TgPI-1 43 and TgPI-1 41 , in tachyzoites, bradyzoites, and sporozoites. TgPI-1 43 and TgPI-1 41 are secreted constitutively from dense granules into the excreted/secreted antigen fraction as well as the parasitophorous vacuole that T. gondii occupies during intracellular replication. Recombinant TgPI-1 inhibits trypsin, chymotrypsin, pancreatic elastase, and neutrophil elastase. Immunoprecipitation studies with anti-rTgPI-1 antibodies reveal that recombinant TgPI-1 forms a complex with trypsin that is dependent on interactions with the active site of the protease. TgPI-1 is the first anti-trypsin/chymotrypsin inhibitor to be identified in bradyzoites and sporozoites, stages of the parasite that would be exposed to proteolytic enzymes in the digestive tract of the host.

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Molecular structure of a Toxoplasma gondii dense granule antigen (GRA 5) associated with the parasitophorous vacuole membrane

Cited by 91 publications

References 28 publications

The microneme protein MIC3 of Toxoplasma gondii is a secretory adhesin that binds to both the surface of the host cells and the surface of the parasite

The microneme protein MIC3 of Toxoplasma gondii is a secretory adhesin that binds to both the surface of the host cells and the surface of the parasite

GRA Proteins of Toxoplasma gondii: Maintenance of Host-Parasite Interactions across the Parasitophorous Vacuolar Membrane

Functional Analysis of Toxoplasma gondii Protease Inhibitor 1

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