Cloning, expression, and primary structure of a Chlamydia trachomatis binding protein.

The gene encoding an 18,000-dalton eucaryotic cell-binding protein of Chlamydia trachomatis serovar L2 was cloned into Escherichia coli, and the nucleotide sequence of a 1,658-base-pair PstI restriction endonuclease fragment encoding this protein was determined. The recombinant chlamydial gene consists of a 486-base-pair open reading frame encoding a polypeptide of molecular weight 18,314. The resultant polypeptide, comprising 162 amino acids, possesses a highly charged carboxy-terminal end. The expression of this recombinant protein is under the control of a vector promoter. The recombinant 18,000-dalton protein possessed the same eucaryotic cell-binding characteristics as did the native chlamydial 18,000-dalton protein when electrophoresed and transferred to nitrocellulose. Polyclonal antibodies to the recombinant protein exhibited neutralizing activity.