Plasmodium yoelii:The Role of the Individual Epidermal Growth Factor-like Domains of the Merozoite Surface Protein-1 in Protection from Malaria

Calvo, Paul A.; Daly, Thomas M.; Long, Carole A.

doi:10.1006/expr.1996.0007

Cited by 14 publications

(11 citation statements)

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“…[26][27][28][29] The expressed mCRISP1 protein in pcDNA-mCRISP1 transfected COS-7 cell line was examined by RT-PCR and indirect immunofluorescence assay. [26][27][28][29] The expressed mCRISP1 protein in pcDNA-mCRISP1 transfected COS-7 cell line was examined by RT-PCR and indirect immunofluorescence assay.…”

Section: Discussionmentioning

confidence: 99%

“…For DNA vaccines, it was important to determine whether it could direct synthesis of the encoded protein correctly in mammalian cells, as it has been confirmed that the configuration of protein is critical for the induction of humoral immune responses. [26][27][28][29] The expressed mCRISP1 protein in pcDNA-mCRISP1 transfected COS-7 cell line was examined by RT-PCR and indirect immunofluorescence assay. RT-PCR results showed that mCRISP1 cDNA positive bands were detected in the pcDNA-mCRISP1 transfected cells and not detected in the pcDNA vector transfected cells and untreated normal cells.…”

Section: Discussionmentioning

confidence: 99%

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Immunogenicity Study of Plasmid DNA Encoding Mouse Cysteine‐Rich Secretory Protein‐1 (mCRISP1) as a Contraceptive Vaccine

Luo

Yang

Cheng

et al. 2012

American J Rep Immunol

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Problem To examine the immunocontraceptive properties of the plasmid pcDNA‐mCRISP1 and compare them to the corresponding recombinant mCRISP1 (r‐mCRISP1). Method of study RT‐PCR and indirect immunofluorescence were performed to observe the mCRISP1 protein expression in COS‐7 cells. Three groups of mice received three injections of r‐mCRISP1, pcDNA‐mCRISP1 or pcDNA vector, respectively. ELISA and Western blot were used to examine the immune responses and immunoreactivity of antisera. Sperm‐egg penetration assay was performed to examine the effect of anti‐mCRISP1 antibodies in vitro fertilization of mouse oocytes. Fertility and mean litter size were analysed by natural mating. Histological analysis was carried out to look for potential immunopathologic effects of the antibodies. Results COS‐7 cells transfected with pcDNA‐mCRISP1 present the expression of mCRISP1. Both r‐mCRISP1 and pcDNA‐mCRISP1 raised an immune response against r‐mCRISP1 protein and native CRISP1 in mouse sperm. The titres of anti‐mCRISP1 antibodies from DNA immunized mice were significantly lower than that of r‐mCRISP1 immunized mice, but it lasted relatively longer. Male and female pcDNA‐mCRISP1 injected animals presented a statistically significant reduction in their fertility with no signs of immunopathologic effects. Conclusion These studies demonstrated the feasibility of generating an immune response to mCRISP1 protein by DNA vaccine and pcDNA‐mCRISP1 plasmid causing significant anti‐fertility potential.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Immunogenicity Study of Plasmid DNA Encoding Mouse Cysteine‐Rich Secretory Protein‐1 (mCRISP1) as a Contraceptive Vaccine

Luo

Yang

Cheng

et al. 2012

American J Rep Immunol

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“…Of these, the carboxyl-terminal 19-kDa fragment, which contains two epidermal growth factor (EGF)-like domains, remains on the surface of the invading merozoite and is carried into the newly invaded erythrocytes (5,7). Antibodies directed against this region are capable of interfering with invasion (5,8,14), animals actively immunized with this region are protected against subsequent challenge (12,23,24), and naturally acquired antibodies to this region are associated with clinical immunity to P. falciparum malaria (19).…”

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confidence: 99%

Structural and Antigenic Properties of Merozoite Surface Protein 4 of Plasmodium falciparum

et al. 1999

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Merozoite surface protein 4 (MSP4) of Plasmodium falciparum is a glycosylphosphatidylinositol-anchored integral membrane protein of 272 residues that possesses a single epidermal growth factor (EGF)-like domain near the carboxyl terminus. We have expressed both full-length MSP4 and a number of fragments inEscherichia coli and have used these recombinant proteins to raise experimental antisera. All recombinant proteins elicited specific antibodies that reacted with parasite-derived MSP4 by immunoblotting. Antibody reactivity was highly dependent on the protein conformation. For example, reduction and alkylation of MSP4 almost completely abolished the reactivity of several antibody preparations, including specificities directed to regions of the protein that do not contain cysteine residues and are far removed from the cysteine-containing EGF-like domain. This indicated the presence of conformation-dependent epitopes in MSP4 and demonstrated that proper folding of the EGF-like domain influenced the antigenicity of the entire molecule. The recombinant proteins were used to map epitopes recognized by individuals living in areas where malaria is endemic, and at least four distinct regions are naturally antigenic during infection. Binding of human antibodies to the EGF-like domain was essentially abrogated after reduction of the recombinant protein, indicating the recognition of conformational epitopes by the human immune responses. This observation led us to examine the importance of conformation dependence in responses to other integral membrane proteins of asexual stages. We analyzed the natural immune responses to a subset of these antigens and demonstrated that there is diminished reactivity to several antigens after reduction. These studies demonstrate the importance of reduction-sensitive structures in the maintenance of the antigenicity of several asexual-stage antigens and in particular the importance of the EGF-like domain in the antigenicity of MSP4.

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“…A number of earlier studies have testified to the powerful nature of the revolutionary approach of DNA vaccinology in malaria (Doolan and Hoffman, 1997;Hoffman et al, 1998;Du et al, 2016). DNA vaccination represents an ideal approach for Previous studies from our lab as well as by other investigators have shown that proper conformation and folding of the PvMSP-142 is critical for the induction of protective humoral immune responses (Dutta et al, 2005;Calvo et al, 1996;Kang et al, 1998). Therefore, it is important to determine initially, before immunization, whether the DNA vaccine construct In the present study we have conducted DNA vaccination for P. vivax MSP-1 42 and compared the immunogenicity of DNA vaccine construct with corresponding protein vaccination in BALB/c mice.…”

Section: Discussionmentioning

confidence: 91%

Immunogenicity of a plasmid DNA vaccine encoding 42 kDa fragment of Plasmodium vivax merozoite surface protein-1

et al. 2016

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Plasmodium yoelii:The Role of the Individual Epidermal Growth Factor-like Domains of the Merozoite Surface Protein-1 in Protection from Malaria

Cited by 14 publications

References 0 publications

Immunogenicity Study of Plasmid DNA Encoding Mouse Cysteine‐Rich Secretory Protein‐1 (mCRISP1) as a Contraceptive Vaccine

Immunogenicity Study of Plasmid DNA Encoding Mouse Cysteine‐Rich Secretory Protein‐1 (mCRISP1) as a Contraceptive Vaccine

Structural and Antigenic Properties of Merozoite Surface Protein 4 of Plasmodium falciparum

Immunogenicity of a plasmid DNA vaccine encoding 42 kDa fragment of Plasmodium vivax merozoite surface protein-1

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