Wong Sandy M, Shaughnessy Jutamas, Ram Sanjay, Akerley Brian J
Department of Microbiology and Immunology, University of Mississippi Medical Center Jackson, MS, USA.
Division of Infectious Diseases and Immunology, University of Massachusetts Medical School Worcester, MA, USA.
Front Cell Infect Microbiol. 2016 Apr 13;6:40. doi: 10.3389/fcimb.2016.00040. eCollection 2016.
Non-typeable Haemophilus influenzae (NTHi) cause a range of illnesses including otitis media, sinusitis, and exacerbation of chronic obstructive pulmonary disease, infections that contribute to the problem of antibiotic resistance and are themselves often intractable to standard antibiotic treatment regimens. We investigated a strategy to exploit binding of the complement inhibitor Factor H (FH) to NTHi as a functional target for an immunotherapeutic containing the NTHi binding domain of FH fused to the Fc domain of IgG1. Chimeric proteins containing the regions that most FH-binding bacteria use to engage human FH, domains 6 and 7 (FH6,7/Fc) and/or 18 through 20 (FH18-20/Fc), were evaluated for binding to NTHi. FH6,7/Fc bound strongly to each of seven NTHi clinical isolates tested and efficiently promoted complement-mediated killing by normal human serum. FH18-20/Fc bound weakly to three of the strains but did not promote complement dependent killing. Outer-membrane protein P5 has been implicated in FH binding by NTHi, and FH6,7/Fc binding was greatly diminished in five of seven P5 deficient isogenic mutant strains tested, implicating an alternative FH binding protein in some strains. Binding of FH18-20/Fc was decreased in the P5 mutant of one strain. A murine model was used to evaluate potential therapeutic application of FH6,7/Fc. FH6,7/Fc efficiently promoted binding of C3 to NTHi exposed to mouse serum, and intranasal delivery of FH6,7/Fc resulted in significantly enhanced clearance of NTHi from the lung. Moreover, a P5 deficient mutant was attenuated for survival in the lung model, suggesting that escape mutants lacking P5 would be less likely to replace strains susceptible to FH6,7/Fc. These results provide evidence for the potential utility of FH6,7/Fc as a therapeutic against NTHi lung infection. FH binding is a common property of many respiratory tract pathogens and FH/Fc chimeras may represent promising alternative or adjunctive therapeutics against such infections, which are often polymicrobial.
不可分型流感嗜血杆菌(NTHi)可引发一系列疾病,包括中耳炎、鼻窦炎以及慢性阻塞性肺疾病急性加重,这些感染加剧了抗生素耐药性问题,且自身往往对标准抗生素治疗方案难以治愈。我们研究了一种策略,利用补体抑制剂因子H(FH)与NTHi的结合作为免疫治疗的功能靶点,该免疫治疗药物包含与IgG1的Fc结构域融合的FH的NTHi结合结构域。评估了包含大多数与FH结合细菌用于结合人FH的区域的嵌合蛋白,即结构域6和7(FH6,7/Fc)以及/或者18至20(FH18 - 20/Fc)与NTHi的结合情况。FH6,7/Fc与所测试的七株NTHi临床分离株中的每一株都紧密结合,并有效促进正常人血清介导的补体杀伤作用。FH18 - 20/Fc与三株菌株结合较弱,且不促进补体依赖性杀伤。外膜蛋白P5被认为与NTHi的FH结合有关,在所测试的七株P5缺陷同基因突变株中的五株中,FH6,7/Fc的结合显著减少,这表明在某些菌株中存在另一种FH结合蛋白。在一株菌株的P5突变体中,FH18 - 20/Fc的结合减少。使用小鼠模型评估FH6,7/Fc的潜在治疗应用。FH6,7/Fc有效促进C3与暴露于小鼠血清中的NTHi的结合,经鼻给药FH6,7/Fc导致肺部NTHi的清除显著增强。此外,一株P5缺陷突变体在肺部模型中的存活能力减弱,这表明缺乏P5的逃逸突变体不太可能取代对FH6,7/Fc敏感的菌株。这些结果为FH6,7/Fc作为治疗NTHi肺部感染的潜在药物提供了证据。FH结合是许多呼吸道病原体的共同特性,FH/Fc嵌合体可能代表针对此类通常为多微生物感染的有前景的替代或辅助治疗方法。