Prokudina E N, Semenova N P, Iamnikova S S
Vopr Virusol. 1989 May-Jun;34(3):280-3.
The capacity of influenza virus nucleoprotein (NP) to bind monoclonal antibodies upon virus treatment with factors affecting the conformation condition of the protein: ultraviolet irradiation, heating to 100 degrees C, acid pH, was studied. Upon the action of these factors NP epitopes demonstrated different time course of inactivation which suggests that they differ in their structural organization and, possibly, in their position in NP. From the possibility of formation in UV-irradiated virus of RNA-protein linkings, the UV-resistant epitope of NP is considered to be most distant from RNA as compared with other epitopes.
研究了流感病毒核蛋白(NP)在用影响蛋白质构象状态的因素(紫外线照射、加热至100摄氏度、酸性pH)处理病毒后与单克隆抗体结合的能力。在这些因素的作用下,NP表位表现出不同的失活时间进程,这表明它们在结构组织上存在差异,并且可能在NP中的位置也不同。从紫外线照射的病毒中可能形成RNA-蛋白质连接来看,与其他表位相比,NP的抗紫外线表位被认为与RNA的距离最远。