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Infection and Immunity, November 1999, p. 5676-5682, Vol. 67, No. 11
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Expression and Characterization of the Mycobacterium tuberculosis Serine/Threonine Protein Kinase PknB

Yossef Av-Gay,* Sarwat Jamil, and Steven J. Drews

Department of Medicine, Division of Infectious Diseases, University of British Columbia, Vancouver, British Columbia, Canada V5Z 3J5

Received 24 June 1999/Returned for modification 29 July 1999/Accepted 26 August 1999

PknB is a member of the newly discovered eukaryotic-like protein serine/threonine kinase (PSTK) family of proteins. The pknB gene was cloned and expressed in Escherichia coli. The active recombinant protein was purified and shown to be reactive with antiphosphoserine antibodies, as well as with antibodies to the phosphorylated eukaryotic Ser/Thr kinases mitogen-activated protein kinase kinase 3 and 6, P38, and Creb. In vitro kinase assays demonstrated that PknB is a functional kinase that is autophosphorylated on serine/threonine residues and is also able to phosphorylate the peptide substrate myelin basic protein. Analysis of pknB expression in Mycobacterium tuberculosis indicates the presence of pknB mRNA in (i) organisms grown in vitro in bacteriological media, (ii) a murine macrophage in vitro infection model, and (iii) in vivo alveolar macrophages from a patient with tuberculosis.

* Corresponding author. Mailing address: Department of Medicine, Division of Infectious Diseases, University of British Columbia, 2733 Heather St., Vancouver, British Columbia, Canada V5Z 3J5. Phone: (604) 875-4588. Fax: (604) 875-4013. E-mail: yossi{at}interchange.ubc.ca.

Infection and Immunity, November 1999, p. 5676-5682, Vol. 67, No. 11
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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