奧地利科學(xué)家日前發(fā)現(xiàn)了黃病毒入侵健康細胞的機理，從而為相關(guān)傳染病的防治研究開辟了新途徑,。
黃病毒是一種微小包膜病毒,，許多傳染病病毒如登革熱病毒、西尼羅河病毒,、流行性乙腦病毒和初夏腦膜炎病毒等都屬于黃病毒科,。
奧地利維也納醫(yī)科大學(xué)病毒醫(yī)學(xué)院的科學(xué)家發(fā)現(xiàn)，黃病毒可以使自己的細胞膜與被感染細胞的細胞膜融合,，通過這種被稱為“受體內(nèi)吞”的機制,，它將自身的遺傳信息植入被感染細胞的細胞質(zhì)中,，從而入侵健康的肌體細胞,。
科學(xué)家還在研究中發(fā)現(xiàn),，一種被稱為“融合蛋白”的物質(zhì)在黃病毒與宿主細胞融合過程中起著關(guān)鍵作用,。這種蛋白對宿主細胞質(zhì)的酸堿程度非常敏感,，宿主細胞質(zhì)的酸性程度越高越有利于黃病毒的入侵。
這一研究成果刊登在最新一期的美國《細胞生物學(xué)》雜志上,。（生物谷Bioon.com）
生物谷推薦原始出處：
The Journal of Cell Biology, Vol. 183, No. 2, 353-361 doi:10.1083/jcb.200806081
Identification of specific histidines as pH sensors in flavivirus membrane fusion
Richard Fritz, Karin Stiasny, and Franz X. Heinz
Institute of Virology, Medical University of Vienna, 1095 Vienna, Austria
The flavivirus membrane fusion machinery, like that of many other enveloped viruses, is triggered by the acidic pH in endosomes after virus uptake by receptor-mediated endocytosis. It has been hypothesized that conserved histidines in the class II fusion protein E of these viruses function as molecular switches and, by their protonation, control the fusion process. Using the mutational analysis of recombinant subviral particles of tick-borne encephalitis virus, we provide direct experimental evidence that the initiation of fusion is crucially dependent on the protonation of one of the conserved histidines (His323) at the interface between domains I and III of E, leading to the dissolution of domain interactions and to the exposure of the fusion peptide. Conserved histidines located outside this critical interface were found to be completely dispensable for triggering fusion.
