The 32-kilodalton envelope protein of vaccinia virus synthesized in Escherichia coli binds with specificity to cell surfaces.
The 32-kilodalton envelope protein of vaccinia virus synthesized in Escherichia coli binds with specificity to cell surfaces.
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在大肠杆菌中合成的痘苗病毒的 32 千道尔顿包膜蛋白与细胞表面特异性结合。
DOI：
10.1128/jvi.65.1.499-504.1991
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发表时间：
1991
影响因子：
5.4
通讯作者：
Esteban,M
中科院分区：
文献类型：
--
作者：
Lai,CF;Gong,SC;Esteban,M
作为病毒感染的第一步，痘苗病毒与宿主细胞表面之间的相互作用的性质尚未确定。一种32 kDa的病毒包膜蛋白已被鉴定为一种细胞表面结合蛋白(J.-S.Maa，J.F.Rodriguez和M.Esteban，J.Biol)。化学。265：1569-1577,1990)。为了研究该蛋白的结构与功能的关系，从含有pT7Ek32表达载体的大肠杆菌中获得了32 kDa的蛋白。重组多肽具有与天然病毒包膜蛋白相似的结构性质。~(125)I标记的32-kDa蛋白与不同来源的培养细胞的结合研究表明，大肠杆菌产生的32-kDa蛋白具有选择性、特异性和饱和性。Scatchard分析表明，每个细胞约有4.5×10(4)个高亲和力位点(Kd=1.8×10(-9)M)，表明32-kDa蛋白与特定受体相互作用。在细菌中大量获得32 kDa病毒蛋白将有助于进一步研究这种病毒包膜蛋白的结构和功能，并有助于鉴定特定的细胞表面受体。
The nature of interaction between vaccinia virus and the surface of host cells as the first step in virus infection is undefined. A 32-kDa virus envelope protein has been identified as a cell surface binding protein (J.-S. Maa, J. F. Rodriguez, and M. Esteban, J. Biol. Chem. 265:1569-1577, 1990). To carry out studies on the structure-function relationship of this protein, the 32-kDa protein was obtained from Escherichia coli cells harboring the expression plasmid pT7Ek32. The recombinant polypeptide was found to have structural properties similar to those of the native virus envelope protein. Binding studies of 125I-labeled 32-kDa protein to cultured cells of various origins revealed that the E. coli-produced 32-kDa protein exhibited selectivity, specificity, and saturability. Scatchard analysis indicated about 4.5 x 10(4) sites per cell with a high affinity (Kd = 1.8 x 10(-9) M), suggesting interaction of the 32-kDa protein with a specific receptor. The availability of large quantities of the 32-kDa virus protein in bacteria will permit further structural and functional studies of this virus envelope protein and facilitate identification of the specific cell surface receptor.
三环类抗抑郁药：治疗血浆水平。
影响因子：
--
作者：
I. Yamashita;Y. Asano
通讯作者：
Y. Asano