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首页> 外文期刊>Infection and immunity >Immunization with Recombinant Transferrin Binding Protein B Enhances Clearance of Nontypeable Haemophilus influenzae from the Rat Lung
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Immunization with Recombinant Transferrin Binding Protein B Enhances Clearance of Nontypeable Haemophilus influenzae from the Rat Lung

机译：重组转铁蛋白结合蛋白B的免疫增强了大鼠肺中不可分型流感嗜血杆菌的清除率

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Nontypeable Haemophilus influenzae (NTHI) is an opportunistic pathogen, and heterogeneity in the surface-exposed immunodominant domains of NTHI proteins is thought to be associated with the failure of an infection to stimulate an immune response that is cross-protective against heterologous NTHI strains. The aim of this study was to assess the vaccine potential of a surface-exposed component of the NTHI human transferrin receptor, TbpB, and to determine if the antibody response elicited was cross-reactive with heterologous strains of NTHI. The efficacy of immunization with a recombinant form of TbpB (rTbpB) was determined by assessing the pulmonary clearance of viable bacteria 4 h after a live challenge with NTHI. There was a significant reduction in the number of viable bacteria in both the bronchoalveolar lavage fluid (34% for the 20-μg dose and 58% for the 40-μg dose) and lung homogenates (26% for the 20-μg dose and 60% for the 40-μg dose) of rats immunized with rTbpB compared to the control animals. While rTbpB-specific antibodies from immunized rats were nonspecific in the recognition of TbpB from six heterologous NTHI strains on Western blots, these antibodies differed in their ability to block transferrin binding to heterologous strains and to cross-react in bactericidal assays. If bactericidal antibodies are key indicators of the efficacy of the immune response in eliminating NTHI, this data suggests that while immunization with rTbpB stimulates protective responses against the homologous isolate, variability in the recognition of TbpB from heterologous isolates may limit the potential of rTbpB as an NTHI vaccine component.
机译：不可分型的流感嗜血杆菌（NTHI）是一种机会病原体，NTHI蛋白表面暴露的免疫优势域的异质性被认为与感染未能激发交叉免疫反应有关。对异源NTHI菌株具有保护作用。这项研究的目的是评估NTHI人类运铁蛋白受体TbpB的表面暴露成分的疫苗潜力，并确定引起的抗体反应是否与NTHI异源菌株交叉反应。用NTHI进行活菌攻击后4小时，通过评估活菌的肺部清除率来确定重组TbpB（rTbpB）免疫的功效。支气管肺泡灌洗液（20μg剂量为34％，40μg剂量为58％）和肺匀浆（20μg剂量和60分别为26％）的活菌数量显着减少与对照组动物相比，使用rTbpB免疫的大鼠（40μg剂量的％）。尽管来自免疫大鼠的rTbpB特异性抗体在Western印迹上对六种异源NTHI菌株对TbpB的识别没有特异性，但这些抗体在阻止转铁蛋白与异源菌株结合以及在细菌测定中交叉反应的能力不同。如果杀菌抗体是消除NTHI的免疫反应功效的关键指标，则该数据表明，尽管用rTbpB进行免疫刺激了针对同源分离株的保护性反应，但异源分离株对TbpB识别的变异性可能会限制rTbpB作为NTHI疫苗成分。

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