Peptides and multiple antigen peptides from <i>Schistosoma mansoni</i> glyceraldehyde 3‐phosphate dehydrogenase: preparation, immunogenicity and immunoprotective capacity in C57BL/6 mice

Vepřek, Pavel; Ježek, Jan; Velek, J.; Tallima, Hatem; Montash, Mona; Ridi, Rashika El

doi:10.1002/psc.550

Cited by 17 publications

(15 citation statements)

References 21 publications

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“…Accordingly, the way was paved to identify the surface membrane antigens of the lung-stage larvae. In this report we show that the vaccine candidate, Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase, SG3PDH (El Ridi et al 2001a, b, 2004a, Vepřek et al 2004 and references therein) is a lung-stage schistosomula surface membrane antigen.…”

Section: Schistosoma Mansoni Glyceraldehyde 3-phosphate Dehydrogenasementioning

confidence: 69%

“…Peptide P5, based on amino acids 178-192 (MTLTYTL NTPTLWPI) of an S. mansoni glucose transporter protein 4 (SGTP4) extrafacial domain (Skelly et al 1998) was synthesized at Harvard Biopolymers Laboratories, Harvard Medical School (Cambridge, MA, USA), and used to prepare an antiserum in BALB/c mice, following procedures previously described (El Ridi et al 2001a, 2004a, Vepřek et al 2004.…”

Section: Methodsmentioning

confidence: 99%

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Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase is a lung-stage schistosomula surface membrane antigen

Tallima¹,

Ridi²

2008

FOLIA PARASIT

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Abstract. We have previously reported that Schistosoma mansoni larvae emerging from host lung at pH 7.5-7.8 and then fixed with diluted formaldehyde (HCHO) readily bind radiation-attenuated cercariae (RA) vaccine serum antibodies, as assessed by indirect membrane immunofluorescence (IF). Here we show that S. mansoni schistosomula emerging from lung pieces under 5% CO 2 (pH ≤7.3) readily bind RA vaccine serum antibodies, provided they have been incubated for 12 h at pH 7.5-7.8 in foetal calf serum-free RPMI medium, and fixed with diluted HCHO. Ex vivo larvae exposed during incubation to GW4869, a specific inhibitor of tegument-bound, neutral sphingomyelinase (nSMase) displayed significantly diminished binding of RA vaccine serum antibodies, thus suggesting that nSMase activity at pH ≥7.5 leads to exposure of lung-stage larvae surface membrane antigens to specific antibody detection. More importantly, ex vivo larvae readily bound antibodies directed to dipeptidic multiple antigen peptide constructs, based on S. mansoni-specific sequences in S. mansoni glyceraldehyde 3-phosphate dehydrogenase (SG3PDH). Lung-stage schistosomula IF reactivity was diminished following antiserum absorption with recombinant SG3PDH. The data together indicate that intact ex vivo, as well as, 5-day-old in vitro-grown larvae express SG3PDH on their surface membrane. The findings are discussed in relation to the importance of surface membrane proteins as candidate vaccine antigens.

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Section: Schistosoma Mansoni Glyceraldehyde 3-phosphate Dehydrogenasementioning

confidence: 69%

Section: Methodsmentioning

confidence: 99%

Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase is a lung-stage schistosomula surface membrane antigen

Tallima¹,

Ridi²

2008

FOLIA PARASIT

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“…In some cases, cDNA clones encoding protective epitopes have been characterized, and the identities of several partially protective antigens are known, including paramyosin (Gobert and McManus 2005), glutathione S-transferase (Capron et al 2005), triose phosphate isomerase (TPI; Harn et al 1992), 14 kDa fatty acid binding protein (Fonseca et al 2006), Sm23 (Da'dara et al 2001Da'dara et al 2002), GAPDH (Argiro et al 2000), and Sm-p80 (Siddiqui et al 2003a;Siddiqui et al 2003b;Siddiqui et al 2005a;Siddiqui et al 2005b). Vaccinations with synthetic or recombinant schistosomal antigens representing selected epitopes have induced partial protection and/or reduced female fecundity in animal models (Balloul et al 1987;Osburn and Stott 1989;Boulanger et al 1991a;Soisson et al 1992;Lebens et al 2003;Tallima et al 2003;Veprek et al 2004). The highest levels of immunity, about 75% protection against cercarial challenge, have been achieved with a truncated portion of a 200 kDa myosin-like protein (rIrV-5) present on the surface of schistosomula (Soisson et al 1992) and with multiple antigenic peptides (MAPs) containing epitopes from either TPI or Sm23 (Harn et al 1995).…”

Section: Vaccine Candidatesmentioning

confidence: 97%

Experimental vaccines in animal models for schistosomiasis

et al. 2008

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Considerable morbidity and mortality results from the affliction of an estimated 200 million people worldwide by several species of schistosomes; 779 million are exposed to the disease in 74 different countries. Even though anti-parasitic drugs and other control measures, including public hygiene and snail control are available, the advent of an effective vaccine still remains the most potentially powerful means for the control of this disease. The putative vaccine could be administered to small children prior to the time when their contact with infected water is maximal, so as to prevent severe infection in the subsequent years. This review attempts to summarize the status of schistosome vaccine development with special emphasis on functionally important vaccine candidates. The importance of utilizing both murine and nonhuman primate models as a prerequisite for clinical trials is discussed.

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“…This may also be the case in trematodes. The extra-cellular location of the enzyme has resulted in trematode GAPDHs receiving considerable attention as vaccine candidates [32][33][34][35][36].…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterisation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from the liver fluke, Fasciola hepatica

Zinsser

Hoey

Trudgett

et al. 2014

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

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Publisher rights This is the author's version of a work that was accepted for publication in Biochimica et Biophysica Acta (BBA) -Proteins and Proteomics. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, vol 1844, issue 4, April 2014. DOI 10.1016/j.bbapap.2014 General rights Copyright for the publications made accessible via the Queen's University Belfast Research Portal is retained by the author(s) and / or other copyright owners and it is a condition of accessing these publications that users recognise and abide by the legal requirements associated with these rights.Take down policy The Research Portal is Queen's institutional repository that provides access to Queen's research output. Every effort has been made to ensure that content in the Research Portal does not infringe any person's rights, or applicable UK laws. If you discover content in the Research Portal that you believe breaches copyright or violates any law, please contact openaccess@qub.ac.uk. Abstract: Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) catalyses one of the two steps in glycolysis which generate the reduced coenzyme NADH. This reaction precedes the two ATP generating steps. Thus, inhibition of GAPDH will lead to substantially reduced energy generation. Consequently, there has been considerable interest in developing GAPDH inhibitors as anti-cancer and anti-parasitic agents. Here, we describe the biochemical characterisation of GAPDH from the common liver fluke Fasciola hepatica (FhGAPDH). The primary sequence of FhGAPDH is similar to that from other trematodes and the predicted structure shows high similarity to those from other animals including the mammalian hosts. FhGAPDH lacks a binding pocket which has been exploited in the design of novel antitrypanosomal compounds. The protein can be expressed in, and purified from Escherichia coli; the recombinant protein was active and showed no cooperativity towards glyceraldehyde 3-phosphate as a substrate. In the absence of ligands, FhGAPDH was a mixture of homodimers and tetramers, as judged by protein-protein crosslinking and analytical gel filtration. The addition of either NAD+ or glyceraldehyde 3-phosphate shifted this equilibrium towards a compact dimer. Thermal scanning fluorimetry demonstrated that this form was considerably more stable than the unliganded one. These responses to ligand binding differ from those seen in mammalian enzymes. These differences could be exploited in the discovery of reagents which selectively disrupt the function of FhGAPDH.Response to Reviewers: Manuscript No.: BBAPRO-14-17 Title: Biochemical characterisation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from the liver fluke, Fasciola hepaticaResponse to Reviewers' ...

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Peptides and multiple antigen peptides from Schistosoma mansoni glyceraldehyde 3‐phosphate dehydrogenase: preparation, immunogenicity and immunoprotective capacity in C57BL/6 mice

Cited by 17 publications

References 21 publications

Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase is a lung-stage schistosomula surface membrane antigen

Schistosoma mansoni glyceraldehyde 3-phosphate dehydrogenase is a lung-stage schistosomula surface membrane antigen

Experimental vaccines in animal models for schistosomiasis

Biochemical characterisation of glyceraldehyde 3-phosphate dehydrogenase (GAPDH) from the liver fluke, Fasciola hepatica

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