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首页> 外文期刊>Infection and immunity >Use of an Isogenic Mutant Constructed inMoraxella catarrhalis To Identify a Protective Epitope of Outer Membrane Protein B1 Defined by Monoclonal Antibody 11C6
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Use of an Isogenic Mutant Constructed inMoraxella catarrhalis To Identify a Protective Epitope of Outer Membrane Protein B1 Defined by Monoclonal Antibody 11C6

机译：使用在卡他莫拉氏菌中构建的同基因突变体来鉴定单克隆抗体11C6定义的外膜蛋白B1的保护性抗原决定簇。

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Moraxella catarrhalis-induced otitis media continues to be a significant cause of infection in young children, prompting increased efforts at identifying effective vaccine antigens. We have previously demonstrated that M. catarrhalis expresses specific outer membrane proteins (OMPs) in response to iron limitation and that this organism can utilize transferrin and lactoferrin for in vitro growth. One of these proteins, which binds human transferrin, is OMP B1. As the human host presents a naturally iron-limited environment, proteins, like OMP B1, which are expressed in response to this nutritional stress are potential vaccine antigens. In this study, we have developed monoclonal antibody (MAb) 11C6, which reacts to a surface-exposed epitope of OMP B1 expressed by M. catarrhalis 7169. This antibody was used to cloneompB1, and sequence analysis suggested that OMP B1 is theM. catarrhalis homologue to the transferrin binding protein B described for pathogenic Neisseriaceae, Haemophilus influenzae, Actinobacillus pleuropneumoniae, andM. catarrhalis. Expression of recombinant OMP B1 on the surface of Escherichia coli confers transferrin binding activity, confirming that this protein is likely involved in iron acquisition. In addition, ompB1 was used to construct an isogenic mutant in M. catarrhalis 7169. This mutant, termed 7169b12, was used as the control in bactericidal assays designed to determine if OMP B1 elicits protective antibodies. In the presence of MAb 11C6 and human complement, wild-type 7169 demonstrated a 99% decline in viability, whereas the ompB1 isogenic mutant was resistant to this bactericidal activity. Further analysis with MAb 11C6 revealed the presence of this OMP B1 epitope on 31% of the clinical isolates tested. These data suggest that OMP B1 is a potential vaccine antigen against M. catarrhalis infections.
机译：卡他莫拉氏菌诱导的中耳炎仍然是幼儿感染的重要原因，促使人们加大了对有效疫苗抗原的鉴定的力度。我们之前已经证明了 M。粘膜炎性皮肤中的卡他alis表达特定的外膜蛋白（OMP），并且该生物体可以利用运铁蛋白和乳铁蛋白进行体外生长。这些与人转铁蛋白结合的蛋白质之一是OMP B1。由于人类宿主呈现天然的铁受限环境，因此响应这种营养压力而表达的蛋白质（如OMP B1）是潜在的疫苗抗原。在这项研究中，我们开发了单克隆抗体（MAb）11C6，它与 M表达的OMP B1的表面暴露表位反应。粘膜炎7169。该抗体被用于克隆 ompB1 ，序列分析表明OMP B1是 M。与致病性奈瑟菌科，流感嗜血杆菌，胸膜肺炎放线杆菌和 M的转铁蛋白结合蛋白B同源。卡他性炎。重组大肠杆菌表面上表达重组OMP B1赋予转铁蛋白结合活性，证实该蛋白可能参与铁的获取。另外，使用 ompB1 在 M中构建一个同基因突变体。粘膜炎7169。此突变体称为7169b12，在旨在确定OMP B1是否引发保护性抗体的杀菌测定中用作对照。在存在单克隆抗体11C6和人类补体的情况下，野生型7169的生存力下降了99％，而 ompB1 等基因突变体则对这种杀菌活性具有抗性。用MAb 11C6进行的进一步分析表明，在测试的31％的临床分离物中存在此OMP B1表位。这些数据表明OMP B1是针对 M的潜在疫苗抗原。卡他氏菌感染。

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