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Journal of Bacteriology, September 2001, p. 5311-5316, Vol. 183, No. 18
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.18.5311-5316.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Microaerophilic Induction of the Alpha-Crystallin
Chaperone Protein Homologue (hspX) mRNA of
Mycobacterium tuberculosis
Lucy E.
DesJardin,1,2,
LaDonna G.
Hayes,3,4
Charles D.
Sohaskey,3
Lawrence G.
Wayne,3,4 and
Kathleen
D.
Eisenach1,2,5,*
Departments of
Pathology1 and
Microbiology/Immunology,5 University of
Arkansas for Medical Sciences, and Central Arkansas
Veterans Healthcare System,2 Little Rock,
Arkansas, and Medical Research Service, Department of
Veterans Affairs Medical Center, Long Beach,3
and Department of Medicine, California College of Medicine,
University of California, Irvine,4 California
Received 19 March 2001/Accepted 11 June 2001
Among the products that are expressed when Mycobacterium
tuberculosis undergoes hypoxic shiftdown to
nonreplicating persistence (NRP) is the alpha-crystallin chaperone
protein homologue (Acr). This expression coincides with the previously
reported appearance of a respiratory type of nitrate reductase
activity, the increase in glycine dehydrogenase activity, and the
production of a unique antigen, URB-1. In a timed sampling study, using
a slowly stirred oxygen depletion culture model, we have demonstrated
that the hspX mRNA that codes for Acr protein as well as
the protein itself is induced just as the bacilli enter the
microaerophilic NRP stage 1 (NRP-1). In contrast to the induction
observed for hspX mRNA, levels of 16S rRNA,
fbpB mRNA (encoding the 85B alpha antigen), and
aroB mRNA (encoding dehydroquinate synthase) demonstrate
relatively small to no change upon entering NRP-1. Acr protein was
shown to be identical to URB-1 by Western analysis with anti-URB-1
antibody. The fact that antibody to Acr is found in a high percentage
of tuberculosis patients suggests that the hypoxic shiftdown of
tubercle bacilli to the NRP state that occurs in vitro, resulting in
production of the alpha-crystallin protein, occurs in vivo as well.
Simultaneous abrupt increases in hspX mRNA and Acr
protein suggest that Acr protein expression is controlled at the level
of transcription.
*
Corresponding author. Mailing address: Central Arkansas
Veterans Healthcare System, Medical Research Service, Slot 151, 4300 W. 7th St., Little Rock, AR 72205-5484. Phone: (501) 257-4827. Fax: (501)
664-6748. E-mail: eisenachkathleend{at}uams.edu.

Present address: University of Iowa, Department of Medicine,
Division of Infectious Diseases and Veterans Affairs Medical
Center,
Iowa City, IA
52246.
Journal of Bacteriology, September 2001, p. 5311-5316, Vol. 183, No. 18
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.18.5311-5316.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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