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J. Biol. Chem., Vol. 278, Issue 20, 18056-18062, May 16, 2003
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From the Protective antigen (PA) is a component of the
Bacillus anthracis lethal and edema toxins and
the basis of the current anthrax vaccine. In its heptameric
form, PA targets host cells and internalizes the enzymatically active
components of the toxins, namely lethal and edema factors. PA and other
toxin components are secreted from B. anthracis using the
Sec-dependent secretion pathway. This requires them to be
translocated across the cytoplasmic membrane in an unfolded state and
then to be folded into their native configurations on the
trans side of the membrane, prior to their release from the
environment of the cell wall. In this study we show that recombinant PA
(rPA) requires the extracellular chaperone PrsA for efficient folding
when produced in the heterologous host, B. subtilis;
increasing the concentration of PrsA leads to an increase in rPA
production. To determine the likelihood of PrsA being required for PA
production in its native host, we have analyzed the B. anthracis genome sequence for the presence of genes encoding
homologues of B. subtilis PrsA. We identified three
putative B. anthracis PrsA proteins (PrsAA, PrsAB, and
PrsAC) that are able to complement the activity of B. subtilis PrsA with respect to cell viability and rPA secretion, as well as that of AmyQ, a protein previously shown to be
PrsA-dependent.
This paper is dedicated to the memory of Dr. Costa Anagnastopoulos, the
father of Bacillus genetics, who died January 2, 2003.
Production of Bacillus anthracis Protective Antigen
Is Dependent on the Extracellular Chaperone, PrsA*
,,,
,,, and**
School of Cell and Molecular Biosciences,
The Medical School, University of Newcastle upon Tyne, Newcastle upon
Tyne, NE2 4HH, United Kingdom, the § Oral Infection and
Immunology Branch, NIDCR, National Institutes of Health, Bethesda,
Maryland 20892, and the Defense Science and Technology
Laboratory, Porton Down, Salisbury SP4 OJQ, United Kingdom
*
This work was supported by grants from the Biotech program
of the European Commission (QLK3-CT-1999-00413), the UK Biotechnology and Biological Research Council, and the Defense Science and Technology Laboratory, UK. The work was carried out within the framework of the
European Bacillus Secretion Group.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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