Changes in acid phosphatase activity during sporulation of Eimeria tenella oocysts

Farooqui, Akhlaq A.; Hanson, William L.

doi:10.1016/0305-0491(83)90059-7

Comparative Biochemistry and Physiology Part B: Comparative Bio

1983

DOI: 10.1016/0305-0491(83)90059-7

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Changes in acid phosphatase activity during sporulation of Eimeria tenella oocysts

Akhlaq A. Farooqui

William L. Hanson

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1987

2003

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Cited by 3 publications

(1 citation statement)

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“…Only a few other biochemical changes in enzymes or proteins during sporulation have been reported. Acid phosphatase may change during the later stages of sporulation of E. tenella (Farooqui and Hanson, 1983), and a heat shock protein (hsp 70) present during sporulation of E. tenella is absent in sporulated oocysts and reexpressed during excystment of sporocysts (Del Cacho et al, 2001). Western blotting studies have shown that expression of 5 E. tenella microneme proteins is developmentally regulated and is coincident with the appearance of these proteins toward the end of sporulation; however, mRNAs for the proteins were detected 10-12 hr earlier (Ryan et al, 2000).…”

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Characterization of a Developmentally Regulated Oocyst Protein From Eimeria Tenella

Fetterer¹,

Barfield²

2003

Journal of Parasitology

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Changes in proteins during sporulation of Eimeria tenella oocysts were investigated. Unsporulated E. tenella oocysts collected from cecal tissue at 7 days postinoculation were sporulated in aerated media at 28 C for 0-48 hr. Gel analysis of soluble protein extracts prepared from oocysts from their respective time points indicated the presence of 2 prominent bands with relative molecular weight (Mr) in the range of 30 kDa and making up 20% of the total protein. These 2 bands, designated as major oocyst proteins (MOPs), were absent or barely detectable by 21 hr of sporulation. MOP bands were weakly reactive with glycoprotein stain but showed no mobility shift on deglycosylation. By gel analysis it was shown that the purified MOPs consisted of 2 bands of Mr 28.7 and 30.1 kDa. However, by matrix-assisted laser deabsorption-time of flight analysis it was shown that masses were about 17% lower. Internal sequence analysis of the 28.7-kDa protein generated 2 peptides of 17 and 14 amino acids in length, consistent with a recently described protein coded by the gam56 gene and expressed in E. maxima gametocytes. Rabbit antibodies made against MOPs were localized to outer portions of sporocysts before excystment and to the apical end of in vitro-derived sporozoites. These same antibodies were found to react with bands of Mr 101 and 65 kDa by Western blot but did not recognize MOPs in soluble or insoluble sporozoite extracts. The data suggest that the MOPs are derived from part of a gametocyte protein similar to that coded by gam56 and are processed during sporulation into sporocyst and sporozoite proteins. Alternatively, the binding of anti-MOP to 101- and 65-kDa proteins may result from alternatively spliced genes as the development of parasite proceeds.

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Characterization of a Developmentally Regulated Oocyst Protein From Eimeria Tenella

Fetterer¹,

Barfield²

2003

Journal of Parasitology

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Comparison of arylsulphatases from Eimeria tenella (parasite) and chicken caecum (host)

Farooqui¹,

Hanson²

1987

Biochemical Journal

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Chicken caecal arylsulphatase was purified 700-fold by (NH4)2SO4 fractionation, concanavalin A-Sepharose and cyclic AMP-Sepharose chromatographies. The purified enzyme was a glycoprotein of Mr 97,000. It hydrolysed p-nitrocatechol sulphate, cerebroside 3-sulphate and ascorbic acid 2-sulphate and was strongly inhibited by Na2SO4 (Ki = 50 microM) and Na3PO4 (Ki = 20 microM). Arylsulphatase from Eimeria tenella sporozoites was purified 28-fold by (NH4)2SO4 fractionation. Arylsulphatase of E. tenella sporozoites was not a glycoprotein. It had an Mr of 49,000. It was inhibited by Na2SO4 (Ki = 300 microM), sodium phosphate (Ki = 90 microM) and heparin. It hydrolysed ascorbic acid 2-sulphate, but cerebroside 3-sulphate was not desulphated. The kinetic parameters of chicken caecal arylsulphatase were different from those of the E. tenella enzyme.

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Studies on the Enzymes of Sarcocystis suicanis: Purification and Characterization of an Acid Phosphatase

Aa¹,

Dd²,

Wl³

et al. 1987

The Journal of Parasitology

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Percoll density gradient centrifugation was used for isolating large quantities of bradyzoites of Sarcocystis suicanis, which were used for enzymatic analysis. Crude extracts of bradyzoites contained activities suggestive of several acid hydrolases. Levels of acid and alkaline phosphatase were higher than those of beta-N-acetylhexosaminidase and beta-galactosidase. Acid phosphatase was purified 156-fold with an overall recovery of 54% using DEAE-Sepharose 4B and Sephadex G-200 chromatography. The partially purified enzyme was not a glycoprotein and had a molecular weight of approximately 170,000. The enzyme was markedly inhibited by Cu++, Hg++, and iodoacetamide, suggesting the presence of a sulfhydryl group. Sodium tartrate caused strong inhibition of the enzyme. The acid phosphatase of S. suicanis appears to be a unique enzyme that cannot be classified under high or low molecular weight acid phosphatases of widely diverse origin.

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Changes in acid phosphatase activity during sporulation of Eimeria tenella oocysts

Cited by 3 publications

References 10 publications

Characterization of a Developmentally Regulated Oocyst Protein From Eimeria Tenella

Characterization of a Developmentally Regulated Oocyst Protein From Eimeria Tenella

Comparison of arylsulphatases from Eimeria tenella (parasite) and chicken caecum (host)

Studies on the Enzymes of Sarcocystis suicanis: Purification and Characterization of an Acid Phosphatase

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