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GRA2 and ROP1 recombinant antigens as potential markers for detection of Toxoplasma gondii-specific immunoglobulin G in humans with acute toxoplasmosis.


ABSTRACT: A goal of the current study was to evaluate serological applications of Toxoplasma gondii GRA2 and rhoptry protein 1 (ROP1) antigens. Soluble recombinant GRA2 and ROP1 antigens as fusion proteins containing six histidyl residues at the N and C terminals were obtained using an Escherichia coli expression system. Purification by one-step metal affinity chromatography allowed recovery of milligram amounts of pure recombinant proteins per liter of culture. The usefulness of these antigens for diagnosis of human infections was tested on 167 serum samples obtained during routine diagnostic tests. A panel of 37 serum samples from patients with acute toxoplasmosis was compared to a panel of 90 serum samples from individuals with past infection. The results indicated that both GRA2 and ROP1 recombinant antigens detected antibodies more frequently in samples from individuals with acute infections (100% and 94.6%, respectively) than in samples from individuals with chronic infections (22.5% and 15.5%, respectively). These results suggest that immunoglobulin G antibodies against GRA2 and ROP1 antigens are produced during the acute stage of toxoplasmosis but are uncommon in the chronic phase of the infection. Hence, these recombinant proteins can be used as specific molecular markers to differentiate between acute and chronic infections.

SUBMITTER: Holec-Gasior L 

PROVIDER: S-EPMC2668274 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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GRA2 and ROP1 recombinant antigens as potential markers for detection of Toxoplasma gondii-specific immunoglobulin G in humans with acute toxoplasmosis.

Holec-Gasior Lucyna L   Kur Józef J   Hiszczyńska-Sawicka Elzbieta E  

Clinical and vaccine immunology : CVI 20090218 4


A goal of the current study was to evaluate serological applications of Toxoplasma gondii GRA2 and rhoptry protein 1 (ROP1) antigens. Soluble recombinant GRA2 and ROP1 antigens as fusion proteins containing six histidyl residues at the N and C terminals were obtained using an Escherichia coli expression system. Purification by one-step metal affinity chromatography allowed recovery of milligram amounts of pure recombinant proteins per liter of culture. The usefulness of these antigens for diagno  ...[more]

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