SYNTHESIS IN ESCHERICHIA-COLI AND IMMUNOLOGICAL CHARACTERIZATION OF A POLYPEPTIDE CONTAINING THE CLEAVAGE SITES ASSOCIATED WITH TRYPSIN ENHANCEMENT OF ROTAVIRUS SA11 INFECTIVITY
SYNTHESIS IN ESCHERICHIA-COLI AND IMMUNOLOGICAL CHARACTERIZATION OF A POLYPEPTIDE CONTAINING THE CLEAVAGE SITES ASSOCIATED WITH TRYPSIN ENHANCEMENT OF ROTAVIRUS SA11 INFECTIVITY
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DOI：
10.1099/0022-1317-68-3-633
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发表时间：
1987-03-01
影响因子：
3.8
通讯作者：
LOPEZ, S
中科院分区：
文献类型：
--
作者：
ARIAS, CF;LIZANO, M;LOPEZ, S
将约45%的轮状病毒SA 11 VP3基因插入到噬菌体λ PL启动子控制的热诱导表达质粒中。基于质粒构建预测的主要翻译产物是杂合蛋白，其中噬菌体MS2聚合酶的98个氨基末端氨基酸之后是VP3蛋白的氨基酸42至387，其包括含有与胰蛋白酶增强感染性相关的切割位点的区域。在诱导时，具有预期mol.重量并含有根据免疫学标准判断的VP3相关氨基酸序列，其合成水平约占细菌总蛋白的15%。当将富含融合多肽的细菌裂解物注射到小鼠中时，它诱导了抑制血凝并中和SA 11轮状病毒感染性的抗体。
About 45% of the rotavirus SA11 VP3 gene was inserted into a thermoinducible expression plasmid under the control of phage lambda PL promoter. The primary translation product predicted on the basis of the plasmid construction was a hybrid protein in which the 98 amino-terminal amino acids of phage MS2 polymerase were followed by amino acids 42 to 387 of the VP3 protein, which included the region containing the cleavage sites associated with trypsin enhancement of infectivity. On induction, a polypeptide that had the expected mol. wt. and contained VP3-related amino acid sequences as judged by immunological criteria, was synthesized to a level representing about 15% of the total bacterial protein. When a bacterial lysate enriched for the fusion polypeptide was injected into mice, it induced antibodies which inhibited haemagglutination and neutralized SA11 rotavirus infectivity.