Malaria vaccine development.

Jones, T R; Hoffman, S L

doi:10.1128/cmr.7.3.303-310.1994

Cited by 4 publications

(5 citation statements)

References 40 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Sub-Saharan Africa depicts a high share (90%) of the global malaria death (WHO 2016). The failure of malaria vector control, due to insecticidal resistance and development of anti-malarial drug resistance, has also resulted in an increase of malaria transmission worldwide, thereby currently receiving intensified attention toward the development of a malaria vaccine (Jones and Hoffman 1994). There are no licensed vaccines available globally so far against malaria.…”

Section: Introductionmentioning

confidence: 99%

Genome-wide identification of novel vaccine candidates for Plasmodium falciparum malaria using integrative bioinformatics approaches

2017

View full text Add to dashboard Cite

In spite of decades of malaria research and clinical trials, a fully effective and long-lasting preventive vaccine remains elusive. In the present study, 5370 proteins of genome were screened for the presence of signal peptide/anchor and GPI anchor motifs. Out of 45 screened surface-associated proteins, 22 were consensually predicted as antigens and had no orthologs in human and mouse except circumsporozoite protein (PF3D7_0304600). Among 22 proteins, 19 were identified as new antigens. In the next step, a total of 4944 peptides were predicted as CD8+ T cell epitopes from 22 probable antigens. Of these, the highest scoring 262 epitopes from each antigen were taken for optimization study in the malaria-endemic regions which covered a broad human population (~93.95%). The predicted epitope 13ILFYFFLWV21 of antigen 6-cysteine (PF3D7_1346800) was binding to the HLA-A*0201 allele with the highest fraction (26%) of immunogenicity in the target populations of North-East Asia, South-East Asia, and sub-Saharan Africa. Therefore, these epitopes are proposed to be favored in vaccine designs against malaria.

show abstract

Section: Introductionmentioning

confidence: 99%

Genome-wide identification of novel vaccine candidates for Plasmodium falciparum malaria using integrative bioinformatics approaches

2017

View full text Add to dashboard Cite

show abstract

“…The deterioriating malaria situation in tropical countries emphasizes the need for new and effective tools for malaria control. In addition to improved strategies for chemotherapy and vector control programmes, an effective malaria vaccine is urgently needed (1,2). Several parasite antigens such as circumsporozoite protein (CSP), C ‐terminal 19 kDa fragment of merozoite surface protein‐1 (MSP‐119), apical membrane antigen‐1 (AMA‐1) and thrombospondin related adhesive protein (TRAP) are now being developed as vaccine target antigens (3–9), and many recombinant multistage vaccines are being studied for their protective efficacy (10,11).…”

Section: Introductionmentioning

confidence: 99%

Immunogenicity of recombinant fragments of Plasmodium falciparum acidic basic repeat antigen produced in Escherichia coli

Kushwaha

Rao

Suresh

et al. 2001

Parasite Immunology

View full text Add to dashboard Cite

The acidic basic repeat antigen (ABRA) of Plasmodium falciparum is a potential vaccine candidate against erythrocytic stages of malaria. We report, for the first time, the immunological characteristics of recombinant ABRA constructs. The recombinant proteins representing different fragments of ABRA were expressed in Escherichia coli, either as fusions with maltose binding protein or as 6X histidine tagged molecules, and purified by affinity chromatography. Immunogenicity studies with these constructs in rabbits and mice indicated that the N-terminal region is the least immunogenic part of ABRA. T-cell proliferation experiments in mice immunized with these constructs revealed that the T-cell epitopes were localized in the middle portion of the protein. More importantly, the purified immunoglobulin G specific to middle and C-terminal fragments prevented parasite growth at levels approaching 80-90%. We found that these proteins were also recognized by sera from P. falciparum-infected patients from Rourkela, a malaria endemic zone of India. Our immunogenicity results suggest that potential of ABRA as a vaccine candidate antigen should be investigated further.

show abstract

“…Many of these determinants are polymorphic and have been suggested to be part of an immune evasion strategy (31,37). On the other hand, P. falciparum repeat domains, such as those found in the circumsporozoite protein, the ring-infected erythrocyte surface antigen, the serine repeat antigen, and merozoite surface protein 2 (MSP-2) may in fact be targets of protective antibodies (27). A second, very different group of potentially protective B-cell epitopes has been mapped to domains of malaria antigens that are conformationally constrained by multiple disulfide bonds.…”

mentioning

confidence: 99%

A Protective Glycosylphosphatidylinositol-Anchored Membrane Protein of Plasmodium yoelii Trophozoites and Merozoites Contains Two Epidermal Growth Factor-Like Domains

2000

View full text Add to dashboard Cite

Using sera from mice immunized and protected against Plasmodium yoelii malaria, we identified a novel blood-stage antigen gene, pypag-2. The 2.1-kb pypag-2 cDNA contains a single open reading frame that encodes a 409-amino-acid protein with a predicted molecular mass of 46.8 kDa. Unlike many characterized plasmodial antigens, blocks of tandemly repeated amino acids are lacking in the pypAg-2 protein sequence. Recombinant pypAg-2, comprising the full-length protein minus the predicted N-terminal signal and C-terminal anchor sequences, was produced and used to raise a high-titer polyclonal rabbit antiserum. This antiserum was used to identify and characterize the native protein through immunoblotting, immunoprecipitation and immunofluorescence assays. Consistent with the presence of a glycosylphosphatidylinositol anchor, pypAg-2 fractionated with the detergent phase of Triton X-114-solubilized proteins and could be metabolically labeled with [ 3 H]palmitic acid. By immunofluorescence, pypAg-2 expression was localized to both the trophozoite and merozoite membranes. Similar to Plasmodium falciparum merozoite surface protein 1, pypAg-2 contains two C-terminal epidermal growth factor (EGF)-like domains. Most importantly, immunization with recombinant pypAg-2 protected mice against lethal P. yoelii malaria. Thus, pypAg-2 is a target of protective immune responses and represents a novel addition to the family of merozoite surface proteins that contain one or more EGF-like domains.

show abstract

Malaria vaccine development.

Cited by 4 publications

References 40 publications

Genome-wide identification of novel vaccine candidates for Plasmodium falciparum malaria using integrative bioinformatics approaches

Genome-wide identification of novel vaccine candidates for Plasmodium falciparum malaria using integrative bioinformatics approaches

Immunogenicity of recombinant fragments of Plasmodium falciparum acidic basic repeat antigen produced in Escherichia coli

A Protective Glycosylphosphatidylinositol-Anchored Membrane Protein of Plasmodium yoelii Trophozoites and Merozoites Contains Two Epidermal Growth Factor-Like Domains

Contact Info

Product

Resources

About