EXPRESSION OF THE B-SUBUNIT OF ESCHERICHIA-COLI HEAT-LABILE ENTEROTOXIN IN A MARINE VIBRIO AND IN A MUTANT THAT IS PLEIOTROPICALLY DEFECTIVE IN THE SECRETION OF EXTRACELLULAR PROTEINS
被引:23
作者:
LEECE, R
论文数: 0引用数: 0
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机构:UNIV LEICESTER, DEPT GENET, LEICESTER LE1 7RH, ENGLAND
LEECE, R
HIRST, TR
论文数: 0引用数: 0
h-index: 0
机构:UNIV LEICESTER, DEPT GENET, LEICESTER LE1 7RH, ENGLAND
HIRST, TR
机构:
[1] UNIV LEICESTER, DEPT GENET, LEICESTER LE1 7RH, ENGLAND
[2] UNIV KENT, BIOL LAB, CANTERBURY CT2 7NJ, ENGLAND
来源:
JOURNAL OF GENERAL MICROBIOLOGY
|
1992年
/
138卷
基金:
英国惠康基金;
关键词:
D O I:
10.1099/00221287-138-4-719
中图分类号:
Q93 [微生物学];
学科分类号:
071005 ;
100705 ;
摘要:
A marine Vibrio (designated Vibrio sp. 60) that is related to Vibrio anguillarum was used as a host for a plasmid that encodes the non-toxic B subunit (EtxB) of Escherichia coli heat-labile enterotoxin. Expression of EtxB in Vibrio sp. 60 resulted in the efficient and selective secretion of the B subunit into the extracellular growth medium. This indicated that Vibrio sp. 60, which does not normally produce cholera-like enterotoxins, nonetheless possesses a secretory machinery that permits these toxins to be translocated across its cytoplasmic and outer membranes. Expression of EtxB in a sec mutant of Vibrio sp. 60 (MVT1192), which had previously been shown to be defective in the secretion of several extracellular proteins, resulted in approximately 95% of the B subunit remaining entrapped within the periplasm of the bacterial cell envelope. This implies that the mutation in MVT1192 defines a locus that determines a common step in the secretion of extracellular proteins, including oligomeric toxins.