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首页> 外文期刊>Vaccine >Vaccine candidate P6 of nontypable Haemophilus influenzae is not a transmembrane protein based on protein structural analysis
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Vaccine candidate P6 of nontypable Haemophilus influenzae is not a transmembrane protein based on protein structural analysis

机译:基于蛋白质结构分析的非典型流感嗜血杆菌的候选疫苗P6不是跨膜蛋白

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P6 has been a vaccine candidate for nontypable Haemophilus influenzae (NTHi) based on its location on the outer membrane and immunogenicity. Because P6 is attached to the inner peptidoglycan layer of NTHi, and is putatively surface exposed, it must be a transmembrane protein. We examined the P6 structure using computational modeling, site-directed mutagenesis, and nuclear magnetic resonance spectroscopy. We found that P6 cannot be a transmembrane protein, and therefore may not be surface exposed. We conclude that there may be another protein on the surface of NTHi that has epitopes similar if not identical to P6
机译:基于其在外膜上的位置和免疫原性,P6已成为不可分型流感嗜血杆菌(NTHi)的候选疫苗。由于P6附着在NTHi的内部肽聚糖层上,并且假定是表面暴露的,因此它必须是跨膜蛋白。我们使用计算模型,定点诱变和核磁共振波谱研究了P6结构。我们发现P6不能是跨膜蛋白,因此可能没有表面暴露。我们得出结论,NTHi表面可能存在另一种具有与P6不同或相似的表位的蛋白质

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