Plasmodium falciparum enolase: stage-specific expression and sub-cellular localization

Bhowmick, Ipsita Pal; Kumar, Nirbhay; Sharma, Shobhona; Coppens, Isabelle; Jarori, Gotam K.

doi:10.1186/1475-2875-8-179

Cited by 63 publications

(66 citation statements)

References 58 publications

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“…[26][27][28][29][30][31][32][33] Independent studies also have implicated externalized α-enolase and GAPDH on mammalian and pathogen surfaces as sites for plasminogen binding and subsequent activation by host or pathogen activities, [26][27][28]30,31,[34][35][36] and we have demonstrated that externalized glycolytic enzymes on the apoptotic cell surface, including α-enolase, also are sites for plasminogen binding. 12 Although enhanced virulence has been attributed to the presumptive augmentation in mobility through matrix or fibrin clots associated with localized plasminogen activation following binding on the pathogen surface, 37,38 no compelling physiological rationale exists for plasminogen binding on non-invasive bacteria and apoptotic cells.…”

Section: Box 1 the Repertoire Of Innate Apoptotic Immunity Early Transupporting

confidence: 58%

Exploiting death: apoptotic immunity in microbial pathogenesis

Ucker

2016

Cell Death Differ

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Innate immunity typically is responsible for initial host responses against infections. Independently, nucleated cells that die normally as part of the physiological process of homeostasis in mammals (including humans) suppress immunity. Specifically, the physiological process of cell death (apoptosis) generates cells that are recognized specifically by viable cells of all types and elicit a profound transient suppression of host immunity (termed 'innate apoptotic immunity' (IAI)). IAI appears to be important normally for the maintenance of self-tolerance and for the resolution of inflammation. In addition, pathogens are able to take advantage of IAI through a variety of distinct mechanisms, to enable their proliferation within the host and enhance pathogenicity. For example, the protist pathogen Leishmania amazonensis, at its infective stage, mimics apoptotic cells by expressing apoptotic-like protein determinants on the cell surface, triggering immunosuppression directly. In contrast, the pathogenic bacterium Listeria monocytogenes triggers cell death in host lymphocytes, relying on those apoptotic cells to suppress host immune control and facilitate bacterial expansion. Finally, although the inhibition of apoptotic cell death is a common attribute of many viruses which facilitates their extended replication, it is clear that adenoviruses also reprogram the non-apoptotic dead cells that arise subsequently to manifest apoptotic-like immunosuppressive properties. These three instances represent diverse strategies used by microbial pathogens to exploit IAI, focusing attention on the potency of this facet of host immune control. Further examination of these cases will be revealing both of varied mechanisms of pathogenesis and the processes involved in IAI control.

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Section: Box 1 the Repertoire Of Innate Apoptotic Immunity Early Transupporting

confidence: 58%

Exploiting death: apoptotic immunity in microbial pathogenesis

Ucker

2016

Cell Death Differ

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“…Surface exposure of glycolytic enzymes has been noted previously in a variety of enteric bacteria and pathogens and is responsible for specific plasminogen binding (17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27). This striking commonality of glycolytic enzyme externalization raises the possibility that the exposure of glycolytic enzymes on microorganisms reflects a subversion of innate apoptotic immunity though apoptotic mimicry that facilitates commensalism or pathogenesis.…”

mentioning

confidence: 74%

Externalized Glycolytic Enzymes Are Novel, Conserved, and Early Biomarkers of Apoptosis

Ucker

Jain

Pattabiraman

et al. 2012

Journal of Biological Chemistry

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Background: Apoptotic cell recognition triggers profound immunosuppressive responses; relevant recognition determinants are uncharacterized. Results: Surface exposure of glycolytic enzymes is a common early apoptotic event. Conclusion: Externalized glycolytic enzyme molecules are novel apoptotic biomarkers and candidate immunomodulatory/ recognition determinants. Significance: Apoptotic glycolytic enzyme externalization explicates plasminogen binding to mammalian cells and potential mechanisms of immune privilege by commensal bacteria and pathogens.

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“…The diverse localization of P. falciparum enolase suggests that, apart from its catalytic activity, it might play other biological roles. For instance, enolase localized on the merozoite surface may be involved in red blood cell invasion, vacuolar enolase (21). Therefore, it seems that many drugs can induce over-expression of enolase in the parasite.…”

Section: Discussionmentioning

confidence: 99%

Caracterización parcial del proteoma del trofozoito de Plasmodium falciparum bajo tratamiento con quinina, mefloquina y el antiplasmodial natural diosgenona

et al. 2014

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Author contributions:Yesid Cuesta-Astroz maintained P. falciparum cultures, prepared protein extracts, carried out 2D electrophoresis and comparative analyses of 2D protein profiles and participated in the preparation of the manuscript. Wanda Maria de Almeida von Krüger optimized the protocols for 2D electrophoresis and protein extracts preparation, revised and edited the manuscript. Mariano Zalis provided the infrastructure for parasite cultivation and participated in the preparation of the manuscript. Paulo Mascarello Bisch optimized the sample preparation protocol for mass spectrometry analysis. Camila Nunes-Batista optimized the conditions to obtain highly synchronized parasite cultures. César Segura conceived, designed and coordinated the study, analyzed the results and wrote the manuscript. All authors read and approved the final manuscript. Objective: The aim of this study was to analyze qualitatively the expression of P.falciparum trophozoite proteins (strain ITG2), after exposure to antimalarial drugs, through a proteomic approach. Partial characterization of Materials and methods:In vitro cultured synchronized parasites were treated with quinine, mefloquine and the natural antiplasmodial diosgenone. Protein extracts were prepared and analyzed by twodimensional electrophoresis. The differentially expressed proteins were selected and identified by MALDI-TOF mass spectrometry. Results:The following proteins were identified among those differentially expressed in the parasite in the presence of the drugs tested: enolase (PF10_0155), calcium-binding protein (PF11_0098), chaperonin (PFL0740c), the host cell invasion protein (PF10_0268) and proteins related to redox processes (MAL8P1.17). These findings are consistent with results of previous studies where the parasite was submitted to pressure with other antimalarial drugs. Conclusion:The observed changes in the P. falciparum trophozoite protein profile induced by antimalarial drugs involved proteins mainly related to the general stress response.

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Plasmodium falciparum enolase: stage-specific expression and sub-cellular localization

Cited by 63 publications

References 58 publications

Exploiting death: apoptotic immunity in microbial pathogenesis

Exploiting death: apoptotic immunity in microbial pathogenesis

Externalized Glycolytic Enzymes Are Novel, Conserved, and Early Biomarkers of Apoptosis

Caracterización parcial del proteoma del trofozoito de Plasmodium falciparum bajo tratamiento con quinina, mefloquina y el antiplasmodial natural diosgenona

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