NDLI: MacAB Is Involved in the Secretion of Escherichia coli Heat-Stable Enterotoxin II▿

Content Provider	PubMed Central
Author	Yamanaka, Hiroyasu Kobayashi, Hidetomo Takahashi, Eizo Okamoto, Keinosuke
Abstract	The heat-stable enterotoxin (ST) produced by enterotoxigenic Escherichia coli is an extracellular peptide toxin that evokes watery diarrhea in the host. Two types of STs, STI and STII, have been found. Both STs are synthesized as precursor proteins and are then converted to the active forms with intramolecular disulfide bonds after being released into the periplasm. The active STs are finally translocated across the outer membrane through a tunnel made by TolC. However, it is unclear how the active STs formed in the periplasm are led to the TolC channel. Several transporters in the inner membrane and their periplasmic accessory proteins are known to combine with TolC and form a tripartite transport system. We therefore expect such transporters to also act as a partner with TolC to export STs from the periplasm to the exterior. In this study, we carried out pulse-chase experiments using E. coli BL21(DE3) mutants in which various transporter genes (acrAB, acrEF, emrAB, emrKY, mdtEF, macAB, and yojHI) had been knocked out and analyzed the secretion of STs in those strains. The results revealed that the extracellular secretion of STII was largely decreased in the macAB mutant and the toxin molecules were accumulated in the periplasm, although the secretion of STI was not affected in any mutant used in this study. The periplasmic stagnation of STII in the macAB mutant was restored by the introduction of pACYC184, containing the macAB gene, into the cell. These results indicate that MacAB, an ATP-binding cassette transporter of MacB and its accessory protein, MacA, participates in the translocation of STII from the periplasm to the exterior. Since it has been reported that MacAB cooperates with TolC, we propose that the MacAB-TolC system captures the periplasmic STII molecules and exports the toxin molecules to the exterior.
Related Links	http://dx.doi.org/10.1128/jb.00853-08
Ending Page	7698
Page Count	6
Starting Page	7693
File Format	PDF
ISSN	00219193
e-ISSN	10985530
Journal	Journal of Bacteriology
Issue Number	23
Volume Number	190
Language	English
Publisher	American Society for Microbiology (ASM)
Publisher Date	2008-12-01
Access Restriction	Open
Rights Holder	American Society for Microbiology (ASM)
Subject Keyword	Molecular Biology Microbiology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Molecular Biology Microbiology

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Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

Extracellular secretion of Escherichia coli heat-stable enterotoxin I across the outer membrane.

Determination of the promoter strength of the gene encoding Escherichia coli heat-stable enterotoxin II.

Fusion of Escherichia coli heat-stable enterotoxin and heat-labile enterotoxin B subunit.

Catabolite repression of Escherichia coli heat-stable enterotoxin activity.

Synthesis of Escherichia coli heat-stable enterotoxin STp as a pre-pro form and role of the pro sequence in secretion.

Specificity of the Type II Secretion Systems of Enterotoxigenic Escherichia coli and Vibrio cholerae for Heat-Labile Enterotoxin and Cholera Toxin▿

Thermoactivation of a periplasmic heat-stable enterotoxin of Escherichia coli.

Enzyme-linked immunosorbent assay for Escherichia coli heat-stable enterotoxin type II.

MacAB Is Involved in the Secretion of Escherichia coli Heat-Stable Enterotoxin II▿

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Disulfide bond formation and secretion of Escherichia coli heat-stable enterotoxin II.

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Fusion of Escherichia coli heat-stable enterotoxin and heat-labile enterotoxin B subunit.

Catabolite repression of Escherichia coli heat-stable enterotoxin activity.

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MacAB Is Involved in the Secretion of Escherichia coli Heat-Stable Enterotoxin II▿