This study showed that the antigenicity of a malarial epitope increased with the length of the epitope when inserted at positions aa26 (amino acid position 26) and aa196, but not at aa213, of the Pseudomonas aeruginosa major outer membrane protein OprF (326 amino acids). Immunization studies showed that a 19-aa epitope was significantly more immunogenic than a 7-aa epitope when inserted at aa26 of OprF, while neither an 11- nor a 19-aa epitope fused to the C-terminus of glutathione S-transferase was immunogenic.
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http://dx.doi.org/10.1016/0378-1097(96)00182-6 | DOI Listing |
Sci Rep
October 2024
Molecular Biology of Malaria and Opportunistic Parasites Research Unit, Department of Parasitology, Faculty of Medicine, Chulalongkorn University, Bangkok, Thailand.
Vaccines (Basel)
July 2024
Centre for translational Medicine and Parasitology, Department of Immunology and Microbiology (ISIM), Faculty of Health and Medical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark.
A vaccine protecting against malaria caused by is urgently needed. The blood-stage invasion complex PCRCR consists of the five malarial proteins PfPTRAMP, PfCSS, PfRipr, PfCyRPA, and PfRH5. As each subcomponent represents an essential and highly conserved antigen, PCRCR is considered a promising vaccine target.
View Article and Find Full Text PDFNat Commun
August 2024
Department of Biochemistry and Chemistry, La Trobe Institute for Molecular Sciences, La Trobe University, Victoria, 3086, Australia.
Apical membrane antigen-1 (AMA1) is a conserved malarial vaccine candidate essential for the formation of tight junctions with the rhoptry neck protein (RON) complex, enabling Plasmodium parasites to invade human erythrocytes, hepatocytes, and mosquito salivary glands. Despite its critical role, extensive surface polymorphisms in AMA1 have led to strain-specific protection, limiting the success of AMA1-based interventions beyond initial clinical trials. Here, we identify an i-body, a humanised single-domain antibody-like molecule that recognises a conserved pan-species conformational epitope in AMA1 with low nanomolar affinity and inhibits the binding of the RON2 ligand to AMA1.
View Article and Find Full Text PDFInt J Mol Sci
June 2024
Department of Life Sciences and Systems Biology, University of Turin, Via Accademia Albertina, 13, 10123 Turin, Italy.
Post-translational modifications (PTMs) are essential for regulating protein functions, influencing various fundamental processes in eukaryotes. These include, but are not limited to, cell signaling, protein trafficking, the epigenetic control of gene expression, and control of the cell cycle, as well as cell proliferation, differentiation, and interactions between cells. In this review, we discuss protein PTMs that play a key role in the malaria parasite biology and its pathogenesis.
View Article and Find Full Text PDFFront Cell Infect Microbiol
May 2024
Malaria Department, Naval Medical Research Command, Silver Spring, MD, United States.
Introduction: Diversity in malarial antigens is an immune evasion mechanism that gives malaria parasites an edge over the host. Immune responses against one variant of a polymorphic antigen are usually not fully effective against other variants due to altered epitopes. This study aimed to evaluate diversity in the Plasmodium falciparum antigens apical membrane antigen 1 (PfAMA1) and circumsporozoite protein (PfCSP) from circulating parasites in a malaria-endemic community in southern Ghana and to determine the effects of polymorphisms on antibody response specificity.
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