Schistosoma japonicum calcium-binding tegumental protein SjTP22.4 immunization confers praziquantel schistosomulumicide and antifecundity effect in mice

Zhang, Zhaoping; Xu, Hongxu; Gan, Wenjia; Zeng, Suxiang; Hu, Xuchu

doi:10.1016/j.vaccine.2012.05.056

Cited by 24 publications

(21 citation statements)

References 42 publications

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“…This species expresses 13 family members, some of which have been shown to elicit IgE-mediated immune responses in the host (Fitzsimmons, et al, 2012, Fitzsimmons, et al, 2007, Webster, et al, 1997. Proteins from this family have also been identified and characterised from other species in the genus Schistosoma, from the Chinese liver fluke Clonorchis sinensis (Huang, et al, 2007, Kim, et al, 2012, Senawong, et al, 2012, Subpipattana, et al, 2012, Vichasri-Grams, et al, 2006, the giant liver fluke Fasciola gigantica and the carcinogenic liver fluke, Opisthorchis viverrini (Fitzsimmons, et al, 2004, Li, et al, 2000, Santiago, et al, 1998, Waine, et al, 1994, Xu, et al, 2014, Zhang, et al, 2012.…”

Section: Introductionmentioning

confidence: 99%

“…While many of the proteins have been localised to the tegument of the worm, their in vivo functions have not been elucidated (Fitzsimmons, et al, 2012, Havercroft, et al, 1990, Huang, et al, 2007, Kim, et al, 2012, Lopes, et al, 2009, Mohamed, et al, 1998, Subpipattana, et al, 2012, Xu, et al, 2014, Zhang, et al, 2012. From the available data it is evident that, despite clear sequence similarities, differences exist between the proteins at the biochemical level.…”

Section: Introductionmentioning

confidence: 99%

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FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Cheung

Thomas

Timson

2016

Experimental Parasitology

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FH22 has been previously identified as a calcium-binding protein from the common liver fluke, Fasciola hepatica. It is part of a family of at least four proteins in this organism which combine an EFhand containing N-terminal domain with a C-terminal dynein light chainlike domain. Here we report further biochemical properties of FH22, which we propose should be renamed FhCaBP1 for consistency with other family members. Molecular modelling predicted that the two domains are linked by a flexible region and that the second EF-hand in the N-terminal domain is most likely the calcium ion binding site. Native gel electrophoresis demonstrated that the protein binds both calcium and manganese ions, but not cadmium, magnesium, strontium, barium, cobalt, copper(II), iron (II), nickel, zinc, lead or potassium ions. Calcium ion binding alters the conformation of the protein and increases its stability towards thermal denaturation. FhCaBP1 is a dimer in solution and calcium ions have no detectable effect on the protein's ability to dimerise. FhCaBP1 binds to the calmodulin antagonists trifluoperazine and chlorpromazine. Overall, the FhCaBP1's biochemical properties are most similar to FhCaBP2 a fact consistent with the close sequence and predicted structural similarity between the two proteins. properties are most similar to FhCaBP2 a fact consistent with the close sequence and predicted structural similarity between the two proteins.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Cheung

Thomas

Timson

2016

Experimental Parasitology

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“…In the case of schistosomiasis, it is well established that praziquantel chemotherapy enhances protective immunity (Bourke et al, 2014;Mutapi et al, 1998). Accordingly, sub-curative praziquantel treatment following immunisation with defined schistosome antigens exhibited synergistic effects in several vaccination trials in mice challenged with Schistosoma mansoni (Dupré et al, 1999;Rofatto et al, 2013) or Schistosoma japonicum (Zhang et al, 2012). Immunotherapy of established infections in conjunction with chemotherapy ("immunochemotherapy"), as attempted in the current study, has been less intensively investigated in any host-pathogen system.…”

Section: Discussionmentioning

confidence: 86%

Immunotherapy with mutated onchocystatin fails to enhance the efficacy of a sub-lethal oxytetracycline regimen against Onchocerca ochengi

Bah

Tanya

Makepeace

2015

Veterinary Parasitology

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“…Despite the fact that good vaccine candidates should reduce worm burden alone, our experiments were designed to allow visualization of the synergistic effect of immunization and chemotherapy on the parasites. Similar approaches have been tested in the past, using parasite extract as antigens (Fallon & Doenhoff, 1995) and have recently been proposed again for other recombinant tegument proteins for S. japonicum (Zhang et al, 2012b). Although these conditions will not be reproduced in human treatment, it is probable that vaccine administration will occur concurrent to chemotherapy treatment.…”

Section: Resultsmentioning

confidence: 97%

Immunization with tegument nucleotidases associated with a subcurative praziquantel treatment reduces worm burden followingSchistosoma mansonichallenge

Rofatto

Araujo-Montoya

Miyasato

et al. 2013

PeerJ

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Schistosomiasis is a debilitating disease caused by flatworm parasites of the Schistosoma genus and remains a high public health impact disease around the world, although effective treatment with Praziquantel (PZQ) has been available since the 1970s. Control of this disease would be greatly improved by the development of a vaccine, which could be combined with chemotherapy. The sequencing of the Schistosoma mansoni transcriptome and genome identified a range of potential vaccine antigens. Among these, three nucleotidases from the tegument of the parasite, presumably involved in purinergic signaling and nucleotide metabolism, were proposed as promising vaccine candidates: an alkaline phosphatase (SmAP), a phosphodiesterase (SmNPP-5) and a diphosphohydrolase (SmNTPDase). Herein, we evaluate the potential of these enzymes as vaccine antigens, with or without subcurative PZQ treatment. Immunization of mice with the recombinant proteins alone or in combination demonstrated that SmAP is the most immunogenic of the three. It induced the highest antibody levels, particularly IgG1, associated with an inflammatory cellular immune response characterized by high TNF-α and a Th17 response, with high IL-17 expression levels. Despite the specific immune response induced, immunization with the isolated or combined proteins did not reduce the worm burden of challenged mice. Nonetheless, immunization with SmAP alone or with the three proteins combined, together with subcurative PZQ chemotherapy was able to reduce the worm burden by around 40%. The immunogenicity and relative exposure of SmAP to the host immune system are discussed, as key factors involved in the apparently synergistic effect of SmAP immunization and subcurative PZQ treatment.

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Schistosoma japonicum calcium-binding tegumental protein SjTP22.4 immunization confers praziquantel schistosomulumicide and antifecundity effect in mice

Cited by 24 publications

References 42 publications

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

FhCaBP1 (FH22): A Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Immunotherapy with mutated onchocystatin fails to enhance the efficacy of a sub-lethal oxytetracycline regimen against Onchocerca ochengi

Immunization with tegument nucleotidases associated with a subcurative praziquantel treatment reduces worm burden followingSchistosoma mansonichallenge

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