Achungu Che Roland, Anong Damian Nota, Shey Robert Adamu, Tabe Cevie Jesenta
Department of Microbiology and Parasitology, Faculty of Science, University of Buea, Buea, Cameroon.
Laboratory of Molecular Parasitology, University of Buea, Buea, Cameroon.
Can J Infect Dis Med Microbiol. 2022 Oct 7;2022:1419998. doi: 10.1155/2022/1419998. eCollection 2022.
Given its global morbidity and mortality rates, malaria continues to be a major public health concern. Despite significant progress in the fight against malaria, efforts to control and eradicate the disease globally are in jeopardy due to lack of a universal vaccine. The conserved short peptide sequences found in Domain I of apical membrane antigen 1 (PfAMA1), which are exposed on the parasite cell surface and in charge of invasion of host cells, make PfAMA1 a promising vaccine candidate antigen. The precise amino acids that make up these conserved short peptides are still unknown, and it is still difficult to pinpoint the molecular processes by which PfAMA1 interacts with the human host cell during invasion. The creation of a universal malaria vaccine based on the AMA1 antigen is challenging due to these knowledge limitations. This study used genome mining techniques to look for these particular short peptides in PfAMA1. Thirty individuals with malaria had blood samples taken using Whatman's filter papers. DNA from the parasite was taken out using the Chelex technique. Domain I of the AMA1 gene was amplified using nested polymerase chain reactions, and the amplified products were removed, purified, and sequenced. The DNA sequence generated was converted into the matching amino acid sequence using bioinformatic techniques. These amino acid sequences were utilized to search for antigenic epitopes, therapeutic targets, and conserved short peptides in Domain I of PfAMA1. The results of this investigation shed important light on the molecular mechanisms behind invasion of host cells, a potential PfAMA1 vaccine antigen sequence, and prospective malaria treatment options in the future. Our work offers fresh information on malaria medication and vaccine research that has not been previously discussed.
鉴于疟疾的全球发病率和死亡率，它仍然是一个主要的公共卫生问题。尽管在抗击疟疾方面取得了重大进展，但由于缺乏通用疫苗，全球控制和根除该疾病的努力正面临危险。顶膜抗原1（PfAMA1）第一结构域中发现的保守短肽序列，暴露于寄生虫细胞表面并负责宿主细胞的入侵，使PfAMA1成为一种有前景的疫苗候选抗原。构成这些保守短肽的精确氨基酸仍然未知，并且仍然难以确定PfAMA1在入侵过程中与人类宿主细胞相互作用的分子过程。由于这些知识限制，基于AMA1抗原开发通用疟疾疫苗具有挑战性。本研究使用基因组挖掘技术在PfAMA1中寻找这些特定的短肽。30名疟疾患者使用Whatman滤纸采集血样。使用Chelex技术提取寄生虫的DNA。使用巢式聚合酶链反应扩增AMA1基因的第一结构域，并去除、纯化和测序扩增产物。使用生物信息学技术将生成的DNA序列转换为匹配的氨基酸序列。这些氨基酸序列用于在PfAMA1的第一结构域中搜索抗原表位、治疗靶点和保守短肽。这项研究的结果为宿主细胞入侵背后的分子机制、潜在的PfAMA1疫苗抗原序列以及未来潜在的疟疾治疗选择提供了重要线索。我们的工作提供了关于疟疾药物和疫苗研究的新信息，这些信息以前未曾讨论过。
