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Infect Immun, June 1998, p. 2999-3002, Vol. 66, No. 6
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Molecular Characterization of Treponema pallidum mcp2, a Putative Chemotaxis Protein Gene

Shermalyn R. Greene and Lola V. Stamm*

Program in Infectious Diseases, Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, North Carolina

Received 16 January 1998/Returned for modification 4 March 1998/Accepted 20 March 1998

The nucleotide sequence of the Treponema pallidum mcp2 gene was determined. mcp2 encodes a 45.8-kDa protein whose deduced amino acid sequence has significant homology with the C-terminal region of bacterial methyl-accepting chemotaxis proteins (MCPs). The Mcp2 N terminus lacks the hydrophobic transmembrane regions present in most MCPs. An Mcp2 fusion protein was strongly reactive with antibody (HC23) to the highly conserved domain of MCPs and with rabbit syphilitic serum. Antibody HC23 reacted with six T. pallidum proteins, including a 45-kDa protein that may correspond to Mcp2. This protein was present in the aqueous phase from T. pallidum cells that were solubilized with Triton X-114 and phase partitioned.

* Corresponding author. Mailing address: Program in Infectious Diseases, Department of Epidemiology, School of Public Health, University of North Carolina, Chapel Hill, NC 27599-7400. Phone: (919) 966-3882. Fax: (919) 966-2089. E-mail: lstamm{at}email.unc.edu.

Infect Immun, June 1998, p. 2999-3002, Vol. 66, No. 6
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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