Proliferative responses of Brugia malayi TPX-1 and its epitopic peptide29–43 in an endemic population of human lymphatic filariasis

Madhumathi, Jayaprakasam; Anugraha, Gandhirajan; Prince, Prabhu Rajaiah; Pradiba, Dhinakar; Kaliraj, Perumal

doi:10.1016/j.micinf.2011.01.008

Cited by 7 publications

(7 citation statements)

References 11 publications

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“…Given its critical role for survival of the parasite in the host, TPX-2 is a potential target for vaccine development. Our group and others ( 24 , 27 , 28 , 40 – 42 ) have previously reported the vaccine potential of TPX. Studies showed that r Bm TRX could confer 62% protection against B. malayi challenge in Mastomys model ( 43 ) and 43–69.5% protection in mouse and jird models ( 27 , 28 ).…”

Section: Discussionmentioning

confidence: 78%

“…Thioredoxin peroxidase (TPX-2) is a highly immunogenic protein within the total secretome of B. malayi ( 37 – 39 ). Several groups including ours have reported the vaccine potential of TPX-2 previously ( 24 , 27 , 28 , 40 – 42 ). In fact, one of our studies showed that a trivalent fusion protein rBm HAX (HSP12.6 + ALT-2 + TPX-2) vaccine conferred 67.5% protection in the mouse model ( 30 ).…”

Section: Introductionmentioning

confidence: 80%

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Evaluating the Vaccine Potential of a Tetravalent Fusion Protein (rBmHAXT) Vaccine Antigen Against Lymphatic Filariasis in a Mouse Model

et al. 2018

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Lymphatic filariasis (LF) is a tropical parasitic infection of human transmitted by mosquitoes. Chronic infection results in severe physical disability in the infected patients. Although several potential vaccine antigens were identified by several groups, there are no licensed prophylactic vaccine to date against this infection in the human. Previous attempts from our laboratory to develop a trivalent prophylactic vaccine against LF showed that >90% protection could be achieved in rodent models. However, this trivalent vaccine gave only 35% protection in non-human primates. The major focus of this study was to develop a tetravalent prophylactic vaccine (rBmHAXT) and test the vaccine potential in a mouse model. We evaluated three different adjuvant formulations; alum, glucopyranosyl lipid adjuvant in stable emulsion (GLA/SE) alum (AL019), and mannosylated chitosan (MCA) to determine the optimum adjuvant formulation for rBmHAXT. Results presented in this study show that rBmHAXT + AL019 gave the highest rate of protection (>88%) against challenge infection, compared to rBmHAXT + AL007 (79%), rBmHAXT + MCA (79%) and controls. Analysis of the immune correlates of protection showed that all three adjuvants elicited high titer of antigen-specific IgG1, IgG2a, and IgG2b antibodies. High number of IFN-γ-producing antigen-specific memory cells were generated in the vaccinated animals irrespective of the adjuvants used. Similarly, spleen cells from rBmHAXT-vaccinated animals secreted IL-4, IL-10, and IFN-γ in response to rBmHAXT suggesting the generation of a balanced Th1/Th2 response. There was also an increase in IL-17-secreting cells in rBmHAXT-vaccinated animals. These findings thus suggest that rBmHAXT + AL019 is a better prophylactic formulation for LF.

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Section: Discussionmentioning

confidence: 78%

Section: Introductionmentioning

confidence: 80%

Evaluating the Vaccine Potential of a Tetravalent Fusion Protein (rBmHAXT) Vaccine Antigen Against Lymphatic Filariasis in a Mouse Model

et al. 2018

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“…Mouse models provide us with the insight into the possible mechanism by which the fi larial nematode can be destroyed (Lawrence & Devaney, 2001). Metabolically active enzymes are highly conserved and hence they share homologous regions with host proteins which may show cross reactivity when developed as vaccines (Madhumathi et al, 2011). The sequence similarity of fi larial TRX and TGA with host proteins is a major drawback towards the exploitation of their potent immunogenicity to be developed as vaccines.…”

Section: Discussionmentioning

confidence: 99%

Effect of muramyl dipeptide and alum adjuvants on immunization with Filarial multi antigen peptide vaccine in mice model

et al. 2016

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SummaryFilarial thioredoxin and transglutaminase are enzymes that are secreted throughout the lifecycle of the parasites which are mandatory for the survival of the parasite. They are reported to be promising vaccine candidates, yet the limitation factors of these proteins to be developed as vaccines is their homology they share with the host proteins. Hence immunodominant epitopes from these proteins were constructed as peptides and immunised in mice model with Muramyl dipeptide (MDP) as adjuvant. Immunodominant epitopic portions from Filarial thioredoxin and transglutaminase which are non-homologous with host proteins were constructed as Multi Antigen Peptide (MAP) and assembled in an inert lysine core. The synthesised MAP was immunised with MDP as adjuvant in Balb/c mice model, humoral and cellular immune response were studied. Antibody titre levels for TT MAP with MDP was in par with alum as adjuvant in mice models. T cell responses of TT MAP with MDP showed a balanced T H 1/T H 2 response. The T H 1 cytokines namely IL-2 and IFN-ɤ were also higher in TT MAP immunised groups with MDP as adjuvant whereas alum immunised groups was T H 2 biased. TT MAP admixed with MDP as adjuvant proves to be safe in mice model. Further vaccination studies are underway in permissive animal models to determine the role of TT MAP with MDP as adjuvant in protective immunity against W. bancrofti and B. malayi infections.

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“…The closely related homolog BmPrx1a (86) (Fig. 8B) could be likewise surface-localized or secreted, as it is antigenic in mice (10) and in humans (154,155). The 1-Cys BmPrx6 has been cloned (44) and patented as a vaccine antigen (U.S. Patent 6,352,836); its ortholog from the dog heartworm Dirofilaria immitis is secreted and has been found in developmental stages and localization patterns similar to the filiarial Prx1a enzymes, above (45).…”

Section: Prxs In Helminthsmentioning

confidence: 99%

“…Prx-based helminth vaccine development has also been pursued. The BmPrx1a gene has been used in a DNA cocktail vaccine efficacious in mice (10) and a peptide derived from a BmPrx1a epitope is strongly immunogenic in mouse and human cell lines, and strongly and selectively immunoreacts to sera from immune and infected individuals (154,155). An FhPrx1a-derived vaccine protected goats from liver damage after Fasciola infection (161), but the FgPrx1b-derived vaccine failed to demonstrate efficacy in buffaloes (211).…”

Section: Prxs As Potential Drug Vaccine or Diagnostic Targetsmentioning

confidence: 99%

Peroxiredoxins in Parasites

Gretes

Poole²,

Karplus³

2012

Antioxidants & Redox Signaling

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Proliferative responses of Brugia malayi TPX-1 and its epitopic peptide29–43 in an endemic population of human lymphatic filariasis

Cited by 7 publications

References 11 publications

Evaluating the Vaccine Potential of a Tetravalent Fusion Protein (rBmHAXT) Vaccine Antigen Against Lymphatic Filariasis in a Mouse Model

Evaluating the Vaccine Potential of a Tetravalent Fusion Protein (rBmHAXT) Vaccine Antigen Against Lymphatic Filariasis in a Mouse Model

Effect of muramyl dipeptide and alum adjuvants on immunization with Filarial multi antigen peptide vaccine in mice model

Peroxiredoxins in Parasites

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