Identification and functional characterization of alpha-enolase from Taenia pisiformis metacestode

Zhang, Shaohua; Guo, Aijiang; Zhu, Xueliang; You, Yanan; Hou, Junling; Wang, Qiuxia; Luo, Xin; Xue-peng, Cai

doi:10.1016/j.actatropica.2015.01.007

Cited by 34 publications

(24 citation statements)

References 41 publications

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“…This suggests that plasminogen-binding proteins are exposed to the larval surface, which could allow them to interact with plasminogen at the host-parasite interface. In addition, both antigenic extracts activated plasminogen and enhanced plasmin generation in the presence of host plasminogen activators (tPA and uPA), results that are consistent with those obtained for other parasites [21,22,[26][27][28][29][30][31]. Plasmin generation by tPA was more effective in the presence of AsL3C, which could be due to the role of this molecule as the main activator responsible for the degradation of fibrin at a vascular level [11].…”

Section: Discussionsupporting

confidence: 84%

Pro-fibrinolytic potential of the third larval stage of Ascaris suum as a possible mechanism facilitating its migration through the host tissues

et al. 2020

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Background: Ascaris roundworms are the parasitic nematodes responsible for causing human and porcine ascariasis. Whereas A. lumbricoides is the most common soil-transmitted helminth infecting humans in the world, A. suum causes important economic losses in the porcine industry. The latter has been proposed as a model for the study of A. lumbricoides since both species are closely related. The third larval stage of these parasites carries out an intriguing and complex hepatopulmonary route through the bloodstream of its hosts. This allows the interaction between larvae and the physiological mechanisms of the hosts circulatory system, such as the fibrinolytic system. Parasite migration has been widely linked to the activation of this system by pathogens that are able to bind plasminogen and enhance plasmin generation. Therefore, the aim of this study was to examine the interaction between the infective third larval stage of A. suum and the host fibrinolytic system as a model of the host-Ascaris spp. relationships. Methods: Infective larvae were obtained after incubating and hatching fertile eggs of A. suum in order to extract their cuticle and excretory/secretory antigens. The ability of both extracts to bind and activate plasminogen, as well as promote plasmin generation were assayed by ELISA and western blot. The location of plasminogen binding on the larval surface was revealed by immunofluorescence. The plasminogen-binding proteins from both antigenic extracts were revealed by two-dimensional electrophoresis and plasminogen-ligand blotting, and identified by mass spectrometry. Results: Cuticle and excretory/secretory antigens from infective larvae of A. suum were able to bind plasminogen and promote plasmin generation in the presence of plasminogen activators. Plasminogen binding was located on the larval surface. Twelve plasminogen-binding proteins were identified in both antigenic extracts. Conclusions: To the best of our knowledge, the present results showed for the first time, the pro-fibrinolytic potential of infective larvae of Ascaris spp., which suggests a novel parasite survival mechanism by facilitating the migration through host tissues.

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Section: Discussionsupporting

confidence: 84%

Pro-fibrinolytic potential of the third larval stage of Ascaris suum as a possible mechanism facilitating its migration through the host tissues

et al. 2020

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“…Moreover, enolase may also be an important candidate antigen for vaccines against pathogen infection (Pal-Bhowmick et al, 2007; Zhang et al, 2015, 2016; Mahana et al, 2016; Membrebe et al, 2016). It has been reported that mice immunized with r-Pfen antigen were strongly protected against infection when challenged with mouse malarial parasite Plasmodium yoelii (Pal-Bhowmick et al, 2007), therefore we also tested the protective properties of B. microti enolase.…”

Section: Discussionmentioning

confidence: 99%

“…Enolase has also been suggested to be a major immunogenic protein with antigenic properties, and could therefore be a suitable candidate vaccine for pathogen infection (Zhang et al, 2015; Mahana et al, 2016; Membrebe et al, 2016). Recently, enolase has been demonstrated satisfactory protective properties against Plasmodium spp.…”

Section: Introductionmentioning

confidence: 99%

Complete Molecular and Immunoprotective Characterization of Babesia microti Enolase

et al. 2017

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The apicomplexan Babesia microti is the primary causative agent of human babesiosis, one of the most broadly distributed tick-borne diseases worldwide. B. microti undergoes a complex lifecycle within both the mammalian host and the tick vector, and employs several different specific molecular mechanisms to enter host cells. Enolase, the key glycolytic enzyme in intracellular glucose metabolism, can also be expressed on the parasite’s outer surface, binds to human plasminogen, and coordinates apicomplexan parasite invasion of host cells, however, it lacks sorting sequences or lipoprotein anchor sites. In the present study, we isolated the coding gene of B. microti enolase (BmEno), expressed it within E. coli and purified the recombinant BmEno protein (rBmEno). Consequently, we confirmed cytoplasmic and surface localization of BmEno via immunofluorescence, and demonstrated that rBmEno catalyzes the dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate. Moreover, our results showed that rBmEno binds to human plasminogen, and that the lysine analog ε-aminocaproic acid significantly inhibited this binding. Furthermore plasminogen bound to rBmEno converts to active plasmin. Additionally, actively immunizing mice with rBmEno could evoke a partial protective immunity against B. microti infection following challenge. In conclusion, B. microti enolase is a multifunctional cytoplasmic protein which is also expressed at the parasitic outer surface, facilitates binding to host plasminogen, and could partially protect hosts against parasite infection.

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“…However, further research is needed in order to confirm ApEno's role during the bacterial infection process of host cells. Enolase has also been identified as an important candidate antigen for vaccines against pathogen infection (25)(26)(27)(28)(29). Therefore, further research is also required to evaluate ApEno's potential as a candidate vaccine target to control anaplasmosis infection.…”

Section: Discussionmentioning

confidence: 99%

Expression, purification, and biological characterization of <i>Anaplasma phagocytophilum</i> enolase

Gao

Chen

Liu

2017

BST

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Identification and functional characterization of alpha-enolase from Taenia pisiformis metacestode

Cited by 34 publications

References 41 publications

Pro-fibrinolytic potential of the third larval stage of Ascaris suum as a possible mechanism facilitating its migration through the host tissues

Pro-fibrinolytic potential of the third larval stage of Ascaris suum as a possible mechanism facilitating its migration through the host tissues

Complete Molecular and Immunoprotective Characterization of Babesia microti Enolase

Expression, purification, and biological characterization of <i>Anaplasma phagocytophilum</i> enolase

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