scholarly journals Biophysical and formulation studies of theSchistosoma mansoniTSP-2 extracellular domain recombinant protein, a lead vaccine candidate antigen for intestinal schistosomiasis

2013 ◽  
Vol 9 (11) ◽  
pp. 2351-2361 ◽  
Author(s):  
Weiqiang Cheng ◽  
Elena Curti ◽  
Wanderson C Rezende ◽  
Clifford Kwityn ◽  
Bin Zhan ◽  
...  
Keyword(s):  
Recombinant Protein ◽  
Vaccine Candidate ◽  
Protein A ◽  
Extracellular Domain ◽  
Intestinal Schistosomiasis ◽  
Vaccine Candidate Antigen ◽  
Candidate Antigen

scholarly journals Extent of polymorphism and selection pressure on the Trypanosoma cruzi vaccine candidate antigen Tc24

2020 ◽  
Vol 13 (10) ◽  
pp. 2663-2672
Author(s):  
Audrey Arnal ◽  
Liliana Villanueva‐Lizama ◽  
Christian Teh‐Poot ◽  
Claudia Herrera ◽  
Eric Dumonteil
Keyword(s):  
Trypanosoma Cruzi ◽  
Selection Pressure ◽  
Vaccine Candidate ◽  
Vaccine Candidate Antigen ◽  
Candidate Antigen

Humoral immune responses against the malaria vaccine candidate antigen Plasmodium vivax AMA-1 and IL-4 gene polymorphisms in individuals living in an endemic area of the Brazilian Amazon

Cytokine ◽  
2015 ◽  
Vol 74 (2) ◽  
pp. 273-278 ◽  
Author(s):  
Franciele Maira Moreira Batista Tomaz ◽  
Adriana Antônia da Cruz Furini ◽  
Marcela Petrolini Capobianco ◽  
Marinete Marins Póvoa ◽  
Pamella Cristina Alves Trindade ◽  
...  
Keyword(s):  
Immune Responses ◽  
Endemic Area ◽  
Malaria Vaccine ◽  
Vaccine Candidate ◽  
Brazilian Amazon ◽  
Humoral Immune ◽  
Humoral Immune Responses ◽  
Vaccine Candidate Antigen ◽  
Malaria Vaccine Candidate ◽  
Candidate Antigen

Malaria vaccine candidate antigen targeting the pre-erythrocytic stage ofPlasmodium falciparumproduced at high level in plants

2014 ◽  
Vol 9 (11) ◽  
pp. 1435-1445 ◽  
Author(s):  
Nadja Voepel ◽  
Alexander Boes ◽  
Güven Edgue ◽  
Veronique Beiss ◽  
Stephanie Kapelski ◽  
...  
Keyword(s):  
Malaria Vaccine ◽  
Vaccine Candidate ◽  
Erythrocytic Stage ◽  
Vaccine Candidate Antigen ◽  
Malaria Vaccine Candidate ◽  
High Level ◽  
Candidate Antigen

scholarly journals RALP1 Is a Rhoptry Neck Erythrocyte-Binding Protein of Plasmodium falciparum Merozoites and a Potential Blood-Stage Vaccine Candidate Antigen

2013 ◽  
Vol 81 (11) ◽  
pp. 4290-4298 ◽  
Author(s):  
Daisuke Ito ◽  
Tomoyuki Hasegawa ◽  
Kazutoyo Miura ◽  
Tsutomu Yamasaki ◽  
Thangavelu U. Arumugam ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Vaccine Candidate ◽  
Binding Protein ◽  
Blood Stage ◽  
Merozoite Invasion ◽  
Free System ◽  
Content Type ◽  
Vaccine Candidate Antigen ◽  
Erythrocyte Binding ◽  
Candidate Antigen

ABSTRACTErythrocyte invasion by merozoites is an obligatory stage ofPlasmodiuminfection and is essential to disease progression. Proteins in the apical organelles of merozoites mediate the invasion of erythrocytes and are potential malaria vaccine candidates. Rhoptry-associated, leucine zipper-like protein 1 (RALP1) ofPlasmodium falciparumwas previously found to be specifically expressed in schizont stages and localized to the rhoptries of merozoites by immunofluorescence assay (IFA). Also, RALP1 has been refractory to gene knockout attempts, suggesting that it is essential for blood-stage parasite survival. These characteristics suggest that RALP1 can be a potential blood-stage vaccine candidate antigen, and here we assessed its potential in this regard. Antibodies were raised against recombinant RALP1 proteins synthesized by using the wheat germ cell-free system. Immunoelectron microscopy demonstrated for the first time that RALP1 is a rhoptry neck protein of merozoites. Moreover, our IFA data showed that RALP1 translocates from the rhoptry neck to the moving junction during merozoite invasion. Growth and invasion inhibition assays revealed that anti-RALP1 antibodies inhibit the invasion of erythrocytes by merozoites. The findings that RALP1 possesses an erythrocyte-binding epitope in the C-terminal region and that anti-RALP1 antibodies disrupt tight-junction formation, are evidence that RALP1 plays an important role during merozoite invasion of erythrocytes. In addition, human sera collected from areas in Thailand and Mali where malaria is endemic recognized this protein. Overall, our findings indicate that RALP1 is a rhoptry neck erythrocyte-binding protein and that it qualifies as a potential blood-stage vaccine candidate.

scholarly journals Purification, Characterization, and Immunogenicity of a Disulfide Cross-Linked Plasmodium vivax Vaccine Candidate Antigen, Merozoite Surface Protein 1, Expressed in Escherichia coli

2001 ◽  
Vol 69 (9) ◽  
pp. 5464-5470 ◽  
Author(s):  
Sheetij Dutta ◽  
Lisa A. Ware ◽  
Arnoldo Barbosa ◽  
Christian F. Ockenhouse ◽  
David E. Lanar
Keyword(s):  
Escherichia Coli ◽  
Plasmodium Vivax ◽  
Vaccine Candidate ◽  
Interleukin 2 ◽  
Surface Protein ◽  
Merozoite Surface Protein ◽  
Malarial Parasite ◽  
Merozoite Surface Protein 1 ◽  
Vaccine Candidate Antigen ◽  
Candidate Antigen

ABSTRACT The Plasmodium vivax merozoite surface protein 1 (MSP-1) 42-kDa fragment (PvMSP-1 p42) is a promising vaccine candidate antigen against the blood stage of the malarial parasite. We have developed a process for the production of this vaccine target, keeping in mind its use in human volunteers. A novel strain, Origami(DE3), of Escherichia coli with mutations in the glutathione and thioredoxin reductase genes yielded 60% more soluble PvMSP-1 p42 than the conventional E. coliBL21(DE3) strain. Recombinant PvMSP-1 p42 was purified to ≥99% purity with a rapid two-step protocol designed for easy scaling up. The final product had a low endotoxin content and was stable in its lyophilized form. PvMSP-1 p42 was found to have the predicted primary and tertiary structures and consisted of a single conformer containing one free cysteine, as predicted. The product was recognized by conformational monoclonal antibodies against P. vivax MSP-1. Immunogenicity studies of PvMSP-1 p42 were carried out with two strains of mice and the adjuvants Montanide ISA51 and Montanide ISA720. Both formulations were found to induce high levels of immunoglobulin G1 (IgG1), IgG2b, and IgG2a antibodies along with low levels of IgG3. Lymphocytes from animals in all the PvMSP-1 p42-immunized groups showed proliferative responses upon stimulation with PvMSP-1 p42; the cytokines interleukin 2 (IL-2), gamma interferon, IL-4, and IL-10 were detected in the culture supernatants. These results indicate that PvMSP-1 p42 in combination with both of the adjuvants elicited cellular and humoral responses in mice.

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