The development of the macrogamete and oocyst wall in Eimeria maxima: immuno-light and electron microscopy

Ferguson, David J. P.; Belli, Sabina I.; Smith, Nicholas C.; Wallach, Michael

doi:10.1016/s0020-7519(03)00185-1

Cited by 74 publications

(140 citation statements)

References 17 publications

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“…4B), a finding consistent with anti-EmGam56 localization within E. maxima macrogametes (13). In contrast, EtGFAT localization was more diffuse, and it is not clear whether the protein is restricted to any specific organelle (Fig.…”

Section: Fig 3 Relative Expression Of Etgfat In Different Developmesupporting

confidence: 62%

“…Microscopic analyses have consistently demonstrated that wall-forming bodies I (WFBI) and II (WFBII) form the outer and inner layers of the oocyst wall, respectively (4,13,32). Furthermore, several proteins have been identified that are detected both in macrogamete WFBs and in the oocyst wall.…”

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confidence: 96%

“…Furthermore, several proteins have been identified that are detected both in macrogamete WFBs and in the oocyst wall. The best characterized of these are EmGam56 and EmGam82, glycoproteins of Eimeria maxima, which are components of WFBII and, accordingly, the inner oocyst wall (13). EmGam56 and EmGam82 are processed into smaller peptides prior to incorporation into the oocyst wall, where proposed cross-linking occurs to ensure the formation of a stable extracellular matrix (5,6).…”

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confidence: 99%

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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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Section: Fig 3 Relative Expression Of Etgfat In Different Developmesupporting

confidence: 62%

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confidence: 96%

mentioning

confidence: 99%

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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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“…Anti-EmAPGA is a protein raised against affinity-purified gametocyte antigens (APGA) of E. maxima that recognizes the wall-forming bodies within the macrogamete and the oocyst wall (5).…”

Section: Fig 1 Apicomplexan Cell Division Flexibility (A)mentioning

confidence: 99%

MORN1 Has a Conserved Role in Asexual and Sexual Development across the Apicomplexa

et al. 2008

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The gene encoding the membrane occupation and recognition nexus protein MORN1 is conserved across the Apicomplexa. In Toxoplasma gondii, MORN1 is associated with the spindle poles, the anterior and posterior rings of the inner membrane complex (IMC). The present study examines the localization of MORN1 during the coccidian development of T. gondii and three Eimeria species (in the definitive host) and erythrocytic schizogony of Plasmodium falciparum. During asexual proliferation, MORN1 is associated with the posterior ring of the IMCs of the multiple daughters forming during T. gondii endopolygeny and schizogony in Eimeria and P. falciparum. Furthermore, the expression of P. falciparum MORN1 protein peaked in late schizogony. These data fit a model with a conserved role for MORN1 during IMC assembly in all variations of asexual development. An important new observation is the reactivity of MORN1 antibody with certain sexual stages in T. gondii and Eimeria species. Here MORN1 is organized as a ring-like structure where the microgametes bud from the microgametocyte while in mature microgametes it is present near the flagellar basal bodies and mitochondrion. These observations suggest a conserved role for MORN1 in both asexual and sexual development across the Apicomplexa.

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“…A veil membrane was observed on the outer surface of the macrogamete of E. stiedai and this structure has been reported in only four other eimerian species, namely E. brunetti (Ferguson et al 1977), E. maxima Ferguson et al 2003) and E. acervulina (Pittilo and Ball 1984) all in the chicken, and E. bakuensis in sheep (Pittilo et al, 1988). The role of the veil in oocyst wall development is at present unknown (Mai et al 2009).…”

Section: Discussionmentioning

confidence: 99%

Observations on oocyst development of Eimeria stiedai in rabbits

Ball

Pittilo

Snow

2014

Acta Parasitologica

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The development of the macrogamete and oocyst wall in Eimeria maxima: immuno-light and electron microscopy

Cited by 74 publications

References 17 publications

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

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

MORN1 Has a Conserved Role in Asexual and Sexual Development across the Apicomplexa

Observations on oocyst development of Eimeria stiedai in rabbits

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