Eimeria tenella sporozoites and merozoites differentially express glycosylphosphatidylinositol-anchored variant surface proteins

Tabarés, E.; Ferguson, David J. P.; Clark, Julie D.; Soon, Puay Eng; Wan, Kiew Lian; Tomley, Fiona M.

doi:10.1016/j.molbiopara.2004.01.013

Cited by 74 publications

(66 citation statements)

References 27 publications

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“…Indirect evidence of EtSAG1 shedding was also provided by the fact that this antigen was obviously present in the microneme fraction used for the immunization of mice, leading to hybridoma 2H10E3. A similar observation was previously made for another GPI-anchored sporozoite surface antigen of E. tenella, EtSAG13, which initially had been characterized as a potential microneme protein, EtMIC6, as it co-purifies with the microneme organelles on sucrose density gradients (Tabares et al 2004;Tomley and Soldati 2001). In the present study, we demonstrated for the first time shedding of EtSAG1 from the surface of intracellular sporozoites by both Western blot analysis and In addition, EtSAG1 could also be seen on the surface of intracellular sporozoites.…”

Section: Discussionsupporting

confidence: 74%

“…EtSAG1 is a GPI-anchored protein which can be released from the sporozoite membrane by treatment with bacterial phosphatidylinositol-specific phospholipase C (Tabares et al 2004). However, antigen shedding was observed by us and others in fluorescent studies of extracellular sporozoites when the sporozoites were fixed on a glass slide after moving time of 10 min.…”

Section: Discussionmentioning

confidence: 99%

“…Further analysis of the same sample by ESI-Q-ToF MS/MS could determine de novo sequences of two peptides. One peptide was derived from the already found 19-kDa sporozoite antigen, but the second one appeared to be derived from the sporozoite surface protein T4 (EtSAG1; Brothers et al 1988;Tabares et al 2004), GeneBank GI 158877 (Fig. 5).…”

Section: Analysis Of Antigen-binding Activity and Specificity Of Antimentioning

confidence: 99%

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Model structure of the immunodominant surface antigen of Eimeria tenella identified as a target for sporozoite-neutralizing monoclonal antibody

Jahn¹,

Matros

Bakulina

et al. 2009

Parasitol Res

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Eimeria tenella is a coccidian parasite of great economical importance for poultry industry. The surface of Eimeria invasive agents, sporozoites and merozoites, is coated with a family of developmentally regulated glycosylphosphatidylinositol (GPI)-linked surface antigens (SAGs), some of them involved in the initiation of the infection process. Using 2D gel electrophoresis followed by mass spectrometry, an antigenic surface protein EtSAG1 (TA4) of E. tenella sporozoites has been identified as a target of neutralizing monoclonal antibody 2H10E3. To clarify the mechanism of invasion inhibition caused by the EtSAG1-specific antibodies, a structural model of EtSAG1 was generated. It appears that "EtSAG fold" does not bear an evolutionary relationship to any known protein structure. The intra- and interchain disulfide bonds could be assigned to certain pairs of six conserved cysteines found in members of the EtSAG protein family. The outward-facing surface of the antigen was found to comprise an expanded positively charged patch, thus suggesting that the parasite invasion process may be initiated by sporozoite attachment to negatively charged sulfated proteoglycans on the surface of the host cell.

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Section: Discussionsupporting

confidence: 74%

Section: Discussionmentioning

confidence: 99%

Section: Analysis Of Antigen-binding Activity and Specificity Of Antimentioning

confidence: 99%

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Model structure of the immunodominant surface antigen of Eimeria tenella identified as a target for sporozoite-neutralizing monoclonal antibody

Jahn¹,

Matros

Bakulina

et al. 2009

Parasitol Res

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“…A manual inspection and curation of the data revealed the presence of numerous surface antigen gene (SAG) proteins, a set of GPI-anchored variant surface antigens that constitute an important family of differentially expressed proteins. Toxoplasma gondii also possesses several SAG families but no homologs to E. tenella SAGs have been found (Tabares et al, 2004). Our orthology analysis is in agreement with this result, however it additionally suggests that SAG proteins are not restricted to E. tenella but are also present as orthologs in E. acervulina and E. maxima.…”

Section: Functional Annotationsupporting

confidence: 89%

Desenvolvimento da plataforma EGene para anotação funcional e integração com banco de dados: aplicação e validação em transcritos de Eimeria spp. de galinha doméstica.

Rangel¹

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“…7). GlcNAc is also an essential substrate for the formation of glycosylphosphatidylinositol-anchored proteins (28,41), which comprise many of the known surface molecules of E. tenella merozoites and sporozoites (40). Here, however, we have focused on the process of Nand O-linked glycosylation and its potential role with known Olinked glycoproteins of gametocytes, such as EtGam56.…”

Section: Discussionmentioning

confidence: 99%

The Glycosylation Pathway of Eimeria tenella Is Upregulated during Gametocyte Development and May Play a Role in Oocyst Wall Formation

et al. 2010

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Sexual-stage glycoproteins of Eimeria are important components of the oocyst wall, a structure that ensures the efficient transmission of these and related parasites. In this study, the primary enzyme in the glycosylation pathway of Eimeria tenella, glucosamine:fructose-6-phosphate aminotransferase (EtGFAT), has been characterized as a macrogamete-specific protein. Although the transcription of EtGFAT was observed early in macrogamete development, protein expression was restricted to mature macrogametes, prior to their conversion into unsporulated oocysts. Genes coding for three other enzymes required for N-acetylgalactosamine (GalNAc) synthesis were also transcribed during E. tenella macrogamete development. Gene transcription of the enzyme responsible for the O-linked transfer of GalNAc to proteins, EtGalNAc-T, was upregulated primarily in unsporulated oocyst stages, and accordingly, a significant increase in GalNAc levels was observed in E. tenella gametocytes and oocysts. Gam56 and Gam82, two well-characterized glycoproteins of Eimeria macrogametes and the oocyst wall, contain high levels of GalNAc and represent probable targets of GalNAc O linkage. It appears that the glycosylation pathway, specifically relating to the formation of GalNAc O links, is dramatically upregulated in E. tenella sexual stages and may play a role in directing a number of macrogamete proteins to the developing oocyst wall.

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Eimeria tenella sporozoites and merozoites differentially express glycosylphosphatidylinositol-anchored variant surface proteins

Cited by 74 publications

References 27 publications

Model structure of the immunodominant surface antigen of Eimeria tenella identified as a target for sporozoite-neutralizing monoclonal antibody

Model structure of the immunodominant surface antigen of Eimeria tenella identified as a target for sporozoite-neutralizing monoclonal antibody

Desenvolvimento da plataforma EGene para anotação funcional e integração com banco de dados: aplicação e validação em transcritos de Eimeria spp. de galinha doméstica.

The Glycosylation Pathway of Eimeria tenella Is Upregulated during Gametocyte Development and May Play a Role in Oocyst Wall Formation

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