The Apical Membrane Antigen 1 (AMA-1) is considered a promising candidate for development of a malaria vaccine against asexual stages of Plasmodium. We recently identified domain II (DII) of Plasmodium vivax AMA-1 (PvAMA-1) as a highly immunogenic region recognised by IgG antibodies present in many individuals during patent infection with P. vivax. The present study was designed to evaluate the immunogenic properties of a bacterial recombinant protein containing PvAMA-1 DII. To accomplish this, the recombinant protein was administered to mice in the presence of each of the following six adjuvants: Complete/Incomplete Freund's Adjuvant (CFA/IFA), aluminium hydroxide (Alum), Quil A, QS21 saponin, CpG-ODN 1826 and TiterMax. We found that recombinant DII was highly immunogenic in BALB/c mice when administered in the presence of any of the tested adjuvants. Importantly, we show that DII-specific antibodies recognised the native AMA-1 protein expressed on the surface of P. vivax merozoites isolated from the blood of infected patients. These results demonstrate that a recombinant protein containing PvAMA-1 DII is immunogenic when administered in different adjuvant formulations, and indicate that this region of the AMA-1 protein should continue to be evaluated as part of a subunit vaccine against vivax malaria.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.vaccine.2010.07.017 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Exploring the dual roles of sec-dependent effectors from Candidatus Liberibacter asiaticus in immunity of citrus plants.
Plant Cell Rep
January 2025
MOE Key Laboratory of Laser Life Science and Institute of Laser Life Science, Guangdong Provincial Key Laboratory of Laser Life Science, Guangzhou Key Laboratory of Spectral Analysis and Functional Probes, College of Biophotonics, School of Optoelectronic Science and Engineering, South China Normal University, Guangzhou, 510631, China.
The three SDEs of CLas were expressed in citrus leaves by AuNPs-PEI mediated transient expression system, and promoted the proliferation of CLas and inhibited citrus immunity. Huanglongbing (HLB) is the most severe bacterial disease of citrus caused by Candidatus Liberibacter asiaticus (CLas). CLas suppress host immune responses and promote infection by sec-dependent effectors (SDEs), thus insight into HLB pathogenesis is urgently needed to develop effective management strategies.
View Article and Find Full Text PDFHuman cancer cells xenografts to assess the efficacy of granulysin-based therapeutics.
Methods Cell Biol
January 2025
Apoptosis, Immunity and Cancer Group, Aragón Health Research Institute (IIS-Aragón), University of Zaragoza, Zaragoza, Spain. Electronic address:
9-kDa Granulysin is a protein present in the granules of human activated cytotoxic T lymphocytes and natural killer cells. It has been shown to exert cytolytic activity against a wide variety of microbes: bacteria, fungi, yeast and protozoa. Recombinant isolated granulysin is also capable of inducing tumor cell death, so it could be used as an anti-tumor therapy.
View Article and Find Full Text PDFHeterologous expression of a recombinant ACE inhibitory peptide LYPVK and its potential antihypertensive action mechanism.
Int J Biol Macromol
January 2025
College of Food Science and Engineering, Ocean University of China, Qingdao 266404, China. Electronic address:
Enzymatic hydrolysis approach is commonly employed for preparation of active peptides, while the limited purity and yield of produced peptides hinder further development of action mechanisms. This study presents the biotechnological approach for the efficient production of recombinant angiotensin converting enzyme (ACE) inhibitory peptide LYPVK and investigates its potential antihypertensive action mechanism. DNA encoding sequence of recombinant peptide was designed to form in tandem, which was expressed in Escherichia coli BL21 (DE3).
View Article and Find Full Text PDFExpression, characterization and anti-colon cancer activity of recombinant ginseng peptides with amino acid tandem repeats.
Protein Expr Purif
January 2025
Engineering Research Center of Western Resource Innovation Medicine Green Manufacturing, Ministry of Education, School of Chemical Engineering, Northwest University, Xi'an, 710069, China; Shaanxi R&D Center of Biomaterials and Fermentation Engineering, School of Chemical Engineering, Northwest University, Xi'an, 710069, China; Biotech. & Biomed. Research Institute, Northwest University, Xi'an, 710069, China. Electronic address:
Ginseng peptides, small molecule active ingredients in ginseng, are mainly extracted naturally or synthesised chemically, but high costs and difficulties hinder further research. In this study, a ginseng hexapeptide FKEHGY, named antitumor peptide 0601 (AT0601) and its five tandem sequence repeats AT0605, were expressed in Bacillus subtilis WB600 for the first time, and the bioactivity study showed that the anticancer activity of AT0605 was even significantly higher than that of AT0601 for colon cancer CT26 cells, with IC50s of 16.82±1.
View Article and Find Full Text PDFBacterial expression, purification and characterization of the human Dectin-1 lectin domain for structural and functional studies.
Protein Expr Purif
January 2025
Tohoku Medical and Pharmaceutical University, 4-4-1 Komatsushima, Aoba-ku, Sendai, Miyagi 981-8558, Japan. Electronic address:
Dectin-1 (CLEC7A), a C-type lectin-like receptor that recognizes β-1,3 glucans, has a key role in the innate immune system. While the lectin domain of mouse Dectin-1 has been solubilized and refolded from inclusion bodies in Escherichia coli, similar refolding of the human Dectin-1 lectin domain is hindered by the formation of misfolded multimers with aberrant intermolecular disulfide bonds. The aim of this study was to develop a method for the large-scale production of the human Dectin-1 lectin domain.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!