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{"title":"Impact of neutrophil‐activating protein conservation on diagnostic tests and vaccine design","authors":"Lídia MD Gonçalves, António J Almeida, Cecília RC Calado","doi":"10.1002/jctb.7755","DOIUrl":null,"url":null,"abstract":"BACKGROUNDThe neutrophil activating protein (NAP) is a highly immunogenic and virulence factor of <jats:italic>Helicobacter pylori</jats:italic>, presenting inflammatory and immunomodulatory activity. Consequently, NAP has been explored as a diagnostic and therapeutic target. However, when evaluating a target protein to design diagnostic methods or vaccines, it is critical to determine the protein conservation among the bacterial population, as well the impact of alterations of amino acid residues on the protein antigenic profile.RESULTSIn the present work, NAP conservation and theoretical antigenicity were determined among 51 sequences from <jats:italic>H. pylori</jats:italic> isolated from patients worldwide. A high NAP conservation (83%) was observed, where 17 amino acid residues, among the 144 residues of the protein, were polymorphic. Alterations at these polymorphic sites had a theoretically low impact on predicted antigenicity, where only 5 NAPs out of 51 NAPs presented a slightly different antigenic profile in relation to the consensus sequence. According to that, it was possible to recognize in western blotting 93% of NAP from different bacteria (<jats:italic>n</jats:italic> = 15) using polyclonal antibodies developed against a specific NAP.CONCLUSIONSIt was predicted that when working with polyclonal antibodies or large NAP fragments for diagnostic and vaccine design, slight variation in protein sequence will have a minimal impact on NAP recognition. However, if a NAP monoclonal antibody or small NAP epitopes are considered, it is critical to select the most conserved and antigenic NAP regions, to maximize the coverage of NAP variants. © 2024 Society of Chemical Industry (SCI).","PeriodicalId":15335,"journal":{"name":"Journal of chemical technology and biotechnology","volume":null,"pages":null},"PeriodicalIF":2.8000,"publicationDate":"2024-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of chemical technology and biotechnology","FirstCategoryId":"5","ListUrlMain":"https://doi.org/10.1002/jctb.7755","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"BIOTECHNOLOGY & APPLIED MICROBIOLOGY","Score":null,"Total":0}
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中性粒细胞活化蛋白保护对诊断测试和疫苗设计的影响
背景中性粒细胞活化蛋白(NAP)是幽门螺杆菌的一种高免疫原性致病因子,具有炎症和免疫调节活性。因此,NAP 一直被视为诊断和治疗的靶标。然而,在评估目标蛋白质以设计诊断方法或疫苗时,关键是要确定蛋白质在细菌群体中的保守性,以及氨基酸残基的改变对蛋白质抗原性的影响。结果在本研究中,确定了从全球患者中分离出的 51 个幽门螺杆菌序列的 NAP 保守性和理论抗原性。结果表明,幽门螺杆菌蛋白的 144 个残基中,有 17 个氨基酸残基具有多态性。理论上,这些多态位点的变化对预测抗原性的影响较小,在 51 个 NAP 中,只有 5 个 NAP 的抗原性与共识序列略有不同。结论据预测,在使用多克隆抗体或大的 NAP 片段进行诊断和疫苗设计时,蛋白质序列的微小变化对 NAP 识别的影响微乎其微。但是,如果考虑使用 NAP 单克隆抗体或小型 NAP 表位,则必须选择最保守和最具抗原性的 NAP 区域,以最大限度地覆盖 NAP 变体。© 2024 化学工业协会(SCI)。
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