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首页> 外文期刊>Infection and immunity >Epitope Structure of the Bordetella pertussis Protein P.69 Pertactin, a Major Vaccine Component and Protective Antigen
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Epitope Structure of the Bordetella pertussis Protein P.69 Pertactin, a Major Vaccine Component and Protective Antigen

机译：百日咳博德特氏菌蛋白P.69百日咳杆菌粘附蛋白，主要疫苗成分和保护性抗原的表位结构

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Bordetella pertussis is reemerging in several countries with a traditionally high vaccine uptake. An analysis of clinical isolates revealed antigenic divergence between vaccine strains and circulating strains with respect to P.69 pertactin. Polymorphisms in P.69 pertactin are mainly limited to regions comprised of amino acid repeats, designated region 1 and region 2. Region 1 flanks the RGD motif, which is involved in adherence. Although antibodies against P.69 pertactin are implicated in protective immunity, little is known about the structure and location of its epitopes. Here we describe the identification by pepscan analysis of the locations of mainly linear epitopes recognized by human sera and mouse monoclonal antibodies (MAbs). A total of 24 epitopes were identified, and of these only 2 were recognized by both MAbs and human antibodies in serum. A number of immunodominant epitopes were identified which were recognized by 78 to 93% of the human sera tested. Blocking experiments indicated the presence of high-avidity human antibodies against conformational epitopes. Human antibodies against linear epitopes had much lower avidities, as they were unable to block MAbs. Pepscan analyses revealed several MAbs which bound to both region 1 and region 2. The two regions are separated by 289 amino acids in the primary structure, and we discuss the possibility that they form a single conformational epitope. Thus, both repeat regions may serve to deflect the immune response targeted to the functional domain of P.69 pertactin. This may explain why the variation in P.69 pertactin is so effective, despite the fact that it is limited to only two small segments of the molecule.
机译：百日咳博德特氏菌在疫苗摄入量高的几个国家/地区正在重新出现。对临床分离株的分析显示，疫苗菌株和循环菌株之间就P.69百日咳杆菌粘附素而言存在抗原差异。 P.69百日咳杆菌粘附蛋白的多态性主要限于由氨基酸重复序列组成的区域，称为区域1和区域2。区域1位于RGD基序的侧面，这与粘附有关。尽管针对P.69粘附素的抗体与保护性免疫有关，但对其表位的结构和位置知之甚少。在这里，我们描述了通过pepscan分析对人血清和小鼠单克隆抗体（MAb）识别的主要线性表位位置的鉴定。总共鉴定了24个表位，其中只有2个被血清中的单克隆抗体和人抗体识别。鉴定了许多免疫显性表位，这些表位被78-93％的人类血清所识别。阻断实验表明存在针对构象表位的高抗人抗体。抗线性表位的人抗体的亲和力要低得多，因为它们无法阻断单克隆抗体。百事可乐分析揭示了几个与区域1和区域2结合的单抗。这两个区域在一级结构中被289个氨基酸隔开，我们讨论了它们形成单个构象表位的可能性。因此，两个重复区域都可以用于偏转针对P.69百日咳杆菌粘附蛋白功能域的免疫反应。这也许可以解释为什么P.69百日咳杆菌粘附素的变异如此有效，尽管事实上它仅限于分子的两个小片段。

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