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Journal of Bacteriology, December 2008, p. 7693-7698, Vol. 190, No. 23
0021-9193/08/$08.00+0     doi:10.1128/JB.00853-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

MacAB Is Involved in the Secretion of Escherichia coli Heat-Stable Enterotoxin II{triangledown}

Hiroyasu Yamanaka,1* Hidetomo Kobayashi,1 Eizo Takahashi,2 and Keinosuke Okamoto2

Laboratory of Molecular Microbiological Science, Faculty of Pharmaceutical Sciences, Hiroshima International University, Hiro-Koshingai, Kure, Hiroshima 737-0112,1 Department of Pharmacogenetics, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University, Okayama 700-8530, Japan2

Received 23 June 2008/ Accepted 11 September 2008

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.

* Corresponding author. Mailing address: Laboratory of Molecular Microbiological Science, Faculty of Pharmaceutical Sciences, Hiroshima International University, Hiro-Koshingai, Kure, Hiroshima 737-0112, Japan. Phone: 81-823-73-8294. Fax: 81-823-73-8981. E-mail: h-yamana{at}ps.hirokoku-u.ac.jp

{triangledown} Published ahead of print on 19 September 2008.

Journal of Bacteriology, December 2008, p. 7693-7698, Vol. 190, No. 23
0021-9193/08/$08.00+0     doi:10.1128/JB.00853-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



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