Eimeria tenella microneme protein EtMIC3: identification, localisation and role in host cell infection

Labbé, M.; Venevelles, Patrick de; Girard-Misguich, Fabienne; Bourdieu, Christiane; Guillaume, Arnaud; Pery, P.

doi:10.1016/j.molbiopara.2004.12.002

Cited by 47 publications

(40 citation statements)

References 45 publications

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“…Third, as discussed above, the MAR domain appears to be restricted to coccidians. Of note, E. tenella is a coccidian that does not spread through tissues and does not form tissuecysts but nevertheless also expresses at least one MCP, EtMIC3 (25). Furthermore, EST and genomic data indicate that more MCPs might be expressed.…”

Section: Discussionmentioning

confidence: 99%

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Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Friedrich

Santos

Liu

et al. 2010

Journal of Biological Chemistry

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Numerous intracellular pathogens exploit cell surface glycoconjugates for host cell recognition and entry. Unlike bacteria and viruses, Toxoplasma gondii and other parasites of the phylum Apicomplexa actively invade host cells, and this process critically depends on adhesins (microneme proteins) released onto the parasite surface from intracellular organelles called micronemes (MIC). The microneme adhesive repeat (MAR) domain of T. gondii MIC1 (TgMIC1) recognizes sialic acid (Sia), a key determinant on the host cell surface for invasion by this pathogen. By complementation and invasion assays, we demonstrate that TgMIC1 is one important player in Sia-dependent invasion and that another novel Sia-binding lectin, designated TgMIC13, is also involved. Using BLAST searches, we identify a family of MAR-containing proteins in enteroparasitic coccidians, a subclass of apicomplexans, including T. gondii, suggesting that all these parasites exploit sialylated glycoconjugates on host cells as determinants for enteric invasion. Furthermore, this protein family might provide a basis for the broad host cell range observed for coccidians that form tissue cysts during chronic infection. Carbohydrate microarray analyses, corroborated by structural considerations, show that TgMIC13, TgMIC1, and its homologue Neospora caninum MIC1 (NcMIC1) share a preference for ␣2-3-over ␣2-6-linked sialyl-N-acetyllactosamine sequences. However, the three lectins also display differences in binding preferences. Intense binding of TgMIC13 to ␣2-9-linked disialyl sequence reported on embryonal cells and relatively strong binding to 4-O-acetylated-Sia found on gut epithelium and binding of NcMIC1 to 6sulfo-sialyl Lewis x might have implications for tissue tropism. Sialic acids (Sias)6 occur abundantly in glycoproteins and glycolipids on the cell surface and are exploited by many viruses and bacteria for attachment and host cell entry. Recognition of carbohydrates and in particular sialylated glycoconjugates is important also for host cell invasion by the Apicomplexa (1-4), a phylum that includes several thousand species of obligate intracellular parasites, among them the Plasmodium spp. causing malaria. Enteroparasitic coccidians are a subclass of Apicomplexa comprising Eimeria spp. responsible for coccidiosis in poultry, Neospora spp. causing neosporosis in cattle, and Toxoplasma, the causative agent of toxoplasmosis in warmblooded animals and humans.The host range and cell type targeted by these parasites vary widely across the phylum. Whereas Plasmodium falciparum merozoites exclusively invade erythrocytes of humans and great apes (5), Toxoplasma gondii tachyzoites (the form of the parasite associated with acute infection) invade an extremely broad range of cell types in humans and virtually all warmblooded animals, enabling rapid establishment of infection in the host and dissemination into deep tissues (6). Information is emerging on the involvement of carbohydrate-protein interactions in this broad host cell recognition (1).Many intracellular...

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Section: Discussionmentioning

confidence: 99%

“…Phylogenetic trees were generated using TREEVIEW. seven MAR domains, in which repeats 3-5 are identical (25). EtMCP2, lying downstream of EtMIC3 on contig 29262, was annotated in silico by comparison with EST data from sporulated oocyst and sporozoite stages.…”

Section: T Gondii Possesses More Than One Sia-binding Factor Involvementioning

confidence: 99%

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Friedrich

Santos

Liu

et al. 2010

Journal of Biological Chemistry

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“…The MDBK cells were grown in DMEM (Invitrogen) with 10% FCS (Invitrogen), 1% sodium pyruvate (Sigma-Aldrich), 1% HEPES (Sigma-Aldrich), 2% L-glutamine (Invitrogen), and 2% penicillin/streptomycin (Invitrogen) at 37°C and 5% CO 2 . The assay was performed essentially as previously described (Labbe et al 2005;Schubert et al 2005). The washed E. tenella sporozoites (freshly isolated or thawed from cryopreservation) were labeled in HBSS (Invitrogen) with 1 μM 5,6-carboxy-succinimidyl-fluoresceine-ester (Invitrogen) for 30-60 min and washed twice with DMEM medium supplemented with 2.5% FCS (Invitrogen).…”

Section: Invasion Inhibition Assaymentioning

confidence: 99%

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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“…We also found in this Eimeria-specific protein dataset two sequences homologous to microneme proteins EtMIC2 and EtMIC3. In agreement with this result, orthologs to EtMIC2 (Blake et al, unpublished data available on GenBank under the accession code CBX60033) and EtMIC3 (Labbe et al, 2005) have also been found in E. maxima. For E. acervulina, we believe our result represents the first description of these proteins, and may suggest that this class of proteins is most probably present in other chicken Eimeria spp.…”

Section: Functional Annotationsupporting

confidence: 71%

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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Eimeria tenella microneme protein EtMIC3: identification, localisation and role in host cell infection

Cited by 47 publications

References 45 publications

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

Members of a Novel Protein Family Containing Microneme Adhesive Repeat Domains Act as Sialic Acid-binding Lectins during Host Cell Invasion by Apicomplexan Parasites

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.

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