In vivo analysis of fibroin heavy chain signal peptide of silkworm Bombyx mori using recombinant baculovirus as vector

文献类型： 外文期刊

第一作者： Wang, SP

作者： Wang, SP;Guo, TQ;Guo, XY;Huang, JT;Lu, CD

作者机构：

关键词： signal peptide;fibroin heavy chain;silkworm;Bombyx mori;recombinant AcMNPV;his-tag;LINKED OLIGOSACCHARIDE CHAINS;AMINO-ACID-SEQUENCE;TRANSGENIC SILKWORMS;SUBUNIT COMBINATION;ELEMENTARY UNIT;CLEAVAGE SITES;GENE;SECRETION;LIGHT;PROTEINS

期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：3.575； 五年影响因子：3.381 ）

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收录情况： SCI

摘要： In order to investigate the functional signal peptide of silkworm fibroin heavy chain (FibH) and the effect of N- and C-terminal parts of FibH on the secretion of FibH in vivo, N- and C-terminal segments of fibh gene were fused with enhanced green fluorescent protein (EGFP) gene. The fused gene was then introduced into silkworm larvae and expressed in silk gland using recombinant AcMNPV (Autographa californica multiple nuclear polyhedrosis virus) as vector. The fluorescence of EGFP was observed with fluorescence microscope. FibH-EGFP fusion proteins extracted from silk gland were analyzed by Western blot. Results showed that the two alpha helices within N-terminal 163 amino acid residues and the C-terminal 61 amino acid residues were not necessary for cleavage of signal peptide and secretion of the fusion protein into silk gland. Then the C-terminal 61 amino acid residues were substituted with a His-tag in the fusion protein to facilitate the purification. N-terminal sequencing of the purified protein showed that the signal cleavage site is between position 21 and 22 amino acid residues. (c) 2006 Elsevier Inc. All rights reserved.

分类号： Q5

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