Hijacking of Host Cellular Functions by the Apicomplexa

Plattner, F.; Soldati‐Favre, Dominique

doi:10.1146/annurev.micro.62.081307.162802

Cited by 115 publications

(79 citation statements)

References 100 publications

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“…During host cell entry, the contents of the micronemes, rhoptries and dense granules are sequentially released (Carruthers and Sibley 1997). All these events lead to the creation of the parasitophorous vacuole within the host cell, in which parasites undergo rapid multiplication (Carruthers and Boothroyd 2007;Plattner and Soldati-Favre 2008;Soldati-Favre 2008;Blader and Saeij 2009). Microneme proteins and their proteolytic trimming fragments are considered to be a major class of cellular adhesins involved in recognition and attachment to host cells Cérède et al 2002;Barragan et al 2005;Carruthers and Tomley 2008;El Hajj et al 2008;Soldati-Favre 2008).…”

Section: Introductionmentioning

confidence: 99%

Toxoplasma gondii secretory proteins bind to sulfated heparin structures

Azzouz¹,

Kamena²,

Laurino³

et al. 2012

Glycobiology

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Toxoplasma gondii is the causative agent of toxoplasmosis, one of the most widespread infections in humans and animals, and is a major opportunistic pathogen in immunocompromised patients. Toxoplasma gondii is unique as it can invade virtually any nucleated cell, although the mechanisms are not completely understood. Parasite attachment to the host cell is a prerequisite for reorientation and penetration and likely requires the recognition of molecules at the host cell surface. It has been reported that the affinity of tachyzoites, the invasive form of T. gondii, for host cells can be inhibited by a variety of soluble-sulfated glycosaminoglycans (GAGs), such as heparan sulfate. Using heparin-functionalized zeolites in the absence of host cells, we visualized heparin-binding sites on the surface of tachyzoites by confocal and atomic force microscopy. Furthermore, we report that protein components of the parasite rhoptry, dense granule and surface bind GAGs. In particular, the proteins ROP2 and ROP4 from the rhoptry, GRA2 from the dense granules and the surface protein SAG1 were found to bind heparin. The binding specificities and affinities of individual parasite proteins for natural heparin and heparin oligosaccharides were determined by a combination of heparin oligosaccharide microarrays and surface plasmon resonance. Our results suggest that interactions between sulfated GAGs and parasite surface antigens contribute to T. gondii attachment to host cell surfaces as well as initiating the invasion process, while rhoptries and dense granule organelles may play an important role during the establishment of the infection and during the life of the parasite inside the parasitophorous vacuole.

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Section: Introductionmentioning

confidence: 99%

Toxoplasma gondii secretory proteins bind to sulfated heparin structures

Azzouz¹,

Kamena²,

Laurino³

et al. 2012

Glycobiology

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“…Infection of immunocompetent patients is normally asymptomatic or causes mild disease, but can be life-threatening in immunocompromised patients or after infection in utero. T. gondii actively invades a wide range of host cells and subverts major cellular functions in its host (Plattner and Soldati-Favre, 2008), including apoptotic signalling (Lüder et al, 2009). Infection with T. gondii renders host cells resistant to a variety of pro-apoptotic signals (Nash et al, 1998;Goebel et al, 1999;Goebel et al, 2001;Molestina et al, 2003;Carmen et al, 2006;Vutova et al, 2007;Hippe et al, 2008) and might also counteract the innate 'suicide' program of parasite-infected cells (Lüder and Gross, 2005).…”

Section: Introductionmentioning

confidence: 99%

Toxoplasma gondiiinfection confers resistance against BimS-induced apoptosis by preventing the activation and mitochondrial targeting of pro-apoptotic Bax

Hippe

Weber

Zhou

et al. 2009

Journal of Cell Science

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seen with regard to their conformational changes, the cytosolto-mitochondria targeting and the oligomerization of Bax but not their cellular protein levels. Blockade of Bax and Bak activation was not mediated by the upregulation of antiapoptotic Bcl-2-like proteins following infection. Further, the BH3-mimetic ABT-737 failed to overcome the Toxoplasmaimposed inhibition of Bim S -triggered apoptosis. These results indicate that T. gondii targets activation of pro-apoptotic Bax and Bak to inhibit the apoptogenic function of mitochondria and to increase host-cell viability. Supplementary material available online at

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“…The apicomplexa include many human and animal pathogens such as Plasmodium (causative agent of malaria) (62), Toxoplasma (parasitic toxoplasmosis disease) (63), and Cryptosporidium (diarrhea in mammals). In the sexual stage, Plasmodium lives in the mosquito host and shows greater activity in electron transport and oxidative phosphorylation (64)(65)(66). While in the asexual stage, the parasite lives in a glucose-rich environment (human blood) and gets sufficient ATP through the glycolysis pathway alone (67,68).…”

Section: Discussionmentioning

confidence: 99%

Genomic Insights into Processes Driving the Infection of Alexandrium tamarense by the Parasitoid Amoebophrya sp

Wohlrab

Glöckner

et al. 2014

Eukaryot Cell

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The regulatory circuits during infection of dinoflagellates by their parasites are largely unknown on the molecular level. Here we provide molecular insights into these infection dynamics. Alexandrium tamarense is one of the most prominent harmful algal bloom dinoflagellates. Its pathogen, the dinoflagellate parasitoid Amoebophrya sp., has been observed to infect and control the blooms of this species. We generated a data set of transcripts from three time points (0, 6, and 96 h) during the infection of this parasite-host system. Assembly of all transcript data from the parasitoid (>900,000 reads/313 Mbp with 454/Roche next-generation sequencing [NGS]) yielded 14,455 contigs, to which we mapped the raw transcript reads of each time point of the infection cycle. We show that particular surface lectins are expressed at the beginning of the infection cycle which likely mediate the attachment to the host cell. In a later phase, signal transduction-related genes together with transmembrane transport and cytoskeleton proteins point to a high integration of processes involved in host recognition, adhesion, and invasion. At the final maturation stage, cell division-and proliferation-related genes were highly expressed, reflecting the fast cell growth and nuclear division of the parasitoid. Our molecular insights into dinoflagellate parasitoid interactions point to general mechanisms also known from other eukaryotic parasites, especially from the Alveolata. These similarities indicate the presence of fundamental processes of parasitoid infection that have remained stable throughout evolution within different phyla.

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Hijacking of Host Cellular Functions by the Apicomplexa

Cited by 115 publications

References 100 publications

Toxoplasma gondii secretory proteins bind to sulfated heparin structures

Toxoplasma gondii secretory proteins bind to sulfated heparin structures

Toxoplasma gondiiinfection confers resistance against BimS-induced apoptosis by preventing the activation and mitochondrial targeting of pro-apoptotic Bax

Genomic Insights into Processes Driving the Infection of Alexandrium tamarense by the Parasitoid Amoebophrya sp

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