Characterization of a genomic region encoding the 32-kDa dense granule antigen of Sarcocystis muris (Apicomplexa)

Freyer, Bernd; Hansner, Thomas; Mehlhorn, Heinz; Rüger, Wolfgang

doi:10.1007/s004360050659

Cited by 4 publications

(2 citation statements)

References 31 publications

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“…S1A). Homologs of these proteins, including Sarcocystis muris DG32 (Freyer et al, 1999), were identified only in Apicomplexa that replicate within a PV (Table 1). Except for Plasmodium spp.…”

Section: Resultsmentioning

confidence: 99%

The Toxoplasma Dense Granule Proteins GRA17 and GRA23 Mediate the Movement of Small Molecules between the Host and the Parasitophorous Vacuole

Gold

Kaplan

Lis

et al. 2015

Cell Host & Microbe

218

249

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Summary Toxoplasma gondii is a protozoan pathogen in the phylum Apicomplexa that resides within an intracellular parasitophorous vacuole (PV) that is selectively permeable to small molecules through unidentified mechanisms. We have identified GRA17 as a Toxoplasma-secreted protein that localizes to the parasitophorous vacuole membrane (PVM) and mediates passive transport of small molecules across the PVM. GRA17 is related to the putative Plasmodium translocon protein EXP2 and conserved across PV-residing Apicomplexa. The PVs of GRA17-deficient parasites have aberrant morphology, reduced permeability to small molecules, and structural instability. GRA17-deficient parasites proliferate slowly and are avirulent in mice. These GRA17-deficient phenotypes are rescued by complementation with Plasmodium EXP2. GRA17 functions synergistically with a related protein, GRA23. Exogenous expression of GRA17 or GRA23 alters the membrane conductance properties of Xenopus oocytes in a manner consistent with a large non-selective pore. Thus, GRA17 and GRA23 provide a molecular basis for PVM permeability and nutrient access.

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Section: Resultsmentioning

confidence: 99%

The Toxoplasma Dense Granule Proteins GRA17 and GRA23 Mediate the Movement of Small Molecules between the Host and the Parasitophorous Vacuole

Gold

Kaplan

Lis

et al. 2015

Cell Host & Microbe

218

249

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show abstract

“…The mammalian lysosomal PPT1 enzyme has a putative homologue in T. gondii (TGME49_097880). This protein is expected to be a dense granule protein based on similarity to a Sarcocystis muris dense granule antigen (64,65). It shares only 12% identity and 40% similarity with the mammalian PPT1 and has no predicted serine hydrolase activity based on its sequence.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Serine Hydrolase Targeted by Acyl-protein Thioesterase Inhibitors in Toxoplasma gondii

Kemp

Rusch²,

Adibekian

et al. 2013

Journal of Biological Chemistry

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Background: S-Palmitoylation is an important reversible modification that involves the action of an acyl-protein thioesterase (APT). Results:We identified an active serine hydrolase (TgASH1) specifically targeted by human APT1 inhibitors in Toxoplasma gondii. Conclusion: TgASH1 is dispensable and cannot be solely responsible for S-depalmitoylation in Apicomplexa. Significance: ␤-Lactone-based APT1 inhibitors hit multiple targets in T. gondii and severely compromise parasite survival.

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Isolation and characterization of a cDNA clone encoding a thiol proteinase of Sarcocystis muris cyst mero` zoites (Apicomplexa)

Hansner¹,

Freyer²,

Mehlhorn

et al. 1999

Parasitology Research

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A cDNA library of Sarcocystis muris cyst merozoites was screened using a digoxigenin-labeled probe. This probe was derived from a 504-bp polymerase-chain-reaction fragment representing part of a thiol proteinase. Several cDNA clones were isolated, one of which (PH08) consists of a nucleotide sequence of 1694 bp and encodes the complete prepropolypeptide of a cathepsin L-like proteinase. PH08 contains an open reading frame of 394 amino acid (aa) residues with a 46-residue signal sequence, which is followed by a 129-residue propeptide and 219 aa residues of the mature enzyme. Two potential glycosylation sites and a putative polyadenylation signal were also identified. The occurrence of the highly conserved interspersed ERFNIN aa motif, not found in cathepsin B-like proteinases, suggests the classification of the enzyme as a cathepsin L-like proteinase. Results worked out in this study will enable production of the recombinant thiol proteinase of S. muris cyst merozoites necessary for study of the substrate specificity as well as other biochemical parameters of this enzyme.

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Characterization of a genomic region encoding the 32-kDa dense granule antigen of Sarcocystis muris (Apicomplexa)

Cited by 4 publications

References 31 publications

The Toxoplasma Dense Granule Proteins GRA17 and GRA23 Mediate the Movement of Small Molecules between the Host and the Parasitophorous Vacuole

The Toxoplasma Dense Granule Proteins GRA17 and GRA23 Mediate the Movement of Small Molecules between the Host and the Parasitophorous Vacuole

Characterization of a Serine Hydrolase Targeted by Acyl-protein Thioesterase Inhibitors in Toxoplasma gondii

Isolation and characterization of a cDNA clone encoding a thiol proteinase of Sarcocystis muris cyst mero` zoites (Apicomplexa)

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