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Identification of an EF-Tu protein that is periplasm-associated and processed in Neisseria gonorrhoeae

Department of Microbiology, University of Texas Southwestern Medical School at Dallas, Dallas, Texas 75235, USA
Rocky Mountain Laboratories, NIAID, NIH, Hamilton, Montana 59840, USA
Division of Biological Sciences, University of Montana, Missoula, Montana 59812, USA

⁴Author for correspondence: Stephen F. Porcella. Tel: +1 214 648 5980. Fax: +1 214 648 5907. e-mail: porcella@utsw.swmed.edu

ABSTRACT

A 44 kDa protein is a dominant component of periplasmic extracts of Neisseria gonorrhoeae. Peptide sequence generated from a cyanogen-bromide-cleaved fragment of this protein indicated sequence homology with elongation factor-Tu (EF-Tu). Polyclonal antiserum was made against the 44 kDa protein purified from periplasm extracts of N. gonorrhoeae. The preabsorbed antiserum was immunoblotted against whole-cell lysates on two-dimensional gels. A 44 kDa protein and a smaller 37 kDa protein were recognized by this antiserum. A N. gonorrhoeae phage DNA library was screened and a clone expressing a 44 kDa protein was identified. The DNA insert in this clone contained several genes homologous to genes contained in the str operon of Escherichia coli. One ORF product with a calculated molecular mass of 43 kDa was highly homologous to the EF-TuA of E. coli. A synthetic peptide antiserum specific for a portion of the C terminus of EF-Tu confirmed that the 37 kDa protein in whole-cell lysates of N. gonorrhoeae was a processed form of EF-Tu. Deletion of the tufA gene homologue in N. gonorrhoeae was attempted but was unsuccessful.

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