Summary: A marine (designated sp. 60) that is related to was used as a host for a plasmid that encodes the non-toxic B subunit (EtxB) of heat-labile enterotoxin. Expression of EtxB in sp. 60 resulted in the efficient and selective secretion of the B subunit into the extracellular growth medium. This indicated that 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 mutant of 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.


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