Micronemes
Mostrando 1-12 de 25 artigos, teses e dissertações.
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1. Characterization of the thrombospondin related anonymous protein 2 (TRAP 2) of the protozoan Neospora caninum in the cell invasion process. / Caracterização da proteína anônima relacionada à trombospondina 2 (TRAP 2) do protozoário Neospora caninum no processo de invasão celular
Neospora caninum é um protozoário Apicomplexa, parasita intracelular obrigatório que possui o cão como hospedeiro definitivo e principalmente os bovinos como hospedeiros intermediários, causando nos primeiros encefalopatia e nos últimos abortos com perda da fertilidade, o que acarreta prejuízos significativos na pecuária mundial. O parasita necessita
Publicado em: 2009
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2. Proteção imunológica contra a formação de cistos cerebrais em camundongos vacinados pela via nasal com proteínas recombinates de Toxoplasma gondii
Toxoplasma gondii is a protozoan parasite which can invade and reside in a wide range of host cells. It can infect all warm-blooded animals, including human being. Parasite invasion is associated with protein secretion from three organelles: micronemes, rhoptries and dense granules. These excreted/secreted antigens were highly immunogenic in humans and roden
Publicado em: 2006
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3. Two Conserved Amino Acid Motifs Mediate Protein Targeting to the Micronemes of the Apicomplexan Parasite Toxoplasma gondii
The micronemal protein 2 (MIC2) of Toxoplasma gondii shares sequence and structural similarities with a series of adhesive molecules of different apicomplexan parasites. These molecules accumulate, through a yet unknown mechanism, in secretory vesicles (micronemes), which together with tubular and membrane structures form the locomotion and invasion machiner
American Society for Microbiology.
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4. Association of microneme antigens of Plasmodium brasilianum merozoites with knobs and other parasite-induced structures in host erythrocytes.
The localization of Plasmodium brasilianum antigens, common to merozoite micronemes and parasite-induced structures in the host erythrocyte, was determined by means of immunogold electron microscopy and monoclonal antibodies directed against blood stages of this parasite. All monoclonal antibodies reacted with micronemes. In addition, some reacted with eithe
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5. Characterization of microneme antigens of Cryptosporidium parvum (Protozoa, Apicomplexa).
Two monoclonal antibodies (MAbs) raised against purified excysted oocysts and sporozoites of cryptosporidium parvum reacted in an immunofluorescence assay with antigens located at the anterior pole of the zoites. On Western blots of purified oocysts, these MAbs reacted with a series of bands between 210 and 40 kDa; several of these bands were recognized by b
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6. Sites of Interaction between Aldolase and Thrombospondin-related Anonymous Protein in Plasmodium
Gliding motility and host cell invasion by apicomplexan parasites are empowered by an acto-myosin motor located underneath the parasite plasma membrane. The motor is connected to host cell receptors through trans-membrane invasins belonging to the thrombospondin-related anonymous protein (TRAP) family. A recent study indicates that aldolase bridges the cytop
The American Society for Cell Biology.
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7. Antibodies against Thrombospondin-Related Anonymous Protein Do Not Inhibit Plasmodium Sporozoite Infectivity In Vivo
Thrombospondin-related anonymous protein (TRAP), a candidate malaria vaccine antigen, is required for Plasmodium sporozoite gliding motility and cell invasion. For the first time, the ability of antibodies against TRAP to inhibit sporozoite infectivity in vivo is evaluated in detail. TRAP contains an A-domain, a well-characterized adhesive motif found in int
American Society for Microbiology.
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8. Release of merozoite dense granules during erythrocyte invasion by Plasmodium knowlesi.
We used immunoelectron microscopy to study the fate of dense granules during the invasion of erythrocytes by Plasmodium knowlesi merozoites. When merozoites entered host cells, dense granules moved to the pellicle, released their contents into the parasitophorous vacuole space, and then moved into fingerlike channels of the vacuole membrane. This is the firs
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9. Micronemal Transport of Plasmodium Ookinete Chitinases to the Electron-Dense Area of the Apical Complex for Extracellular Secretion
Plasmodium ookinetes secrete chitinases to penetrate the acellular, chitin-containing peritrophic matrix of the mosquito midgut en route to invasion of the epithelium. Chitinases are potentially targets that can be used to block malaria transmission. We demonstrate here that chitinases of Plasmodium falciparum and P. gallinaceum are concentrated at the apica
American Society for Microbiology.
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10. Neospora caninum Microneme Protein NcMIC3: Secretion, Subcellular Localization, and Functional Involvement in Host Cell Interaction
In apicomplexan parasites, host cell adhesion and subsequent invasion involve the sequential release of molecules originating from secretory organelles named micronemes, rhoptries, and dense granules. Microneme proteins have been shown to be released at the onset of the initial contact between the parasite and the host cell and thus mediate and establish the
American Society for Microbiology.
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11. Rapid invasion of host cells by Toxoplasma requires secretion of the MIC2–M2AP adhesive protein complex
Vertebrate cells are highly susceptible to infection by obligate intracellular parasites such as Toxoplasma gondii, yet the mechanism by which these microbes breach the confines of their target cell is poorly understood. While it is thought that Toxoplasma actively invades by secreting adhesive proteins from internal organelles called micronemes, no genetic
Oxford University Press.
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12. Characterization of a Plasmodium falciparum erythrocyte-binding protein paralogous to EBA-175
A member of a Plasmodium receptor family for erythrocyte invasion was identified on chromosome 13 from the Plasmodium falciparum genome sequence of the Sanger Centre (Cambridge, U.K.). The protein (named BAEBL) has homology to EBA-175, a P. falciparum receptor that binds specifically to sialic acid and the peptide backbone of glycophorin A on erythrocy
The National Academy of Sciences.