Abstract
The Chlamydia trachomatis serovar A hyp operon was cloned, sequenced, and expressed in Escherichia coli. Two cotranscribed open reading frames, hypA and hypB, encoded polypeptides of 17 and 57 kilodaltons, respectively. The deduced amino acid sequences of serovar A HypA and HypB proteins were (respectively) 85 and 94% identical with HypA and HypB proteins of Chlamydia psittaci GPIC, and HypB was greater than 50% identical to 60-kilodalton stress response proteins from other procaryotes and eucaryotes. The sequence should be useful in defining the antigenic structure of the Chlamydia trachomatis HypB protein, a necessary step toward understanding the relationship between the immune response to this protein and the pathogenesis of human chlamydial diseases.
MeSH Terms
Amino Acid Sequence
Bacterial Proteins/genetics
Base Sequence
Chlamydia trachomatis/classification,genetics
Cloning, Molecular
Electrophoresis, Polyacrylamide Gel
Escherichia coli/classification,genetics
Gene Expression
Heat-Shock Proteins/genetics
Molecular Sequence Data
Operon
Recombinant Fusion Proteins/genetics
Sequence Homology, Nucleic Acid
Chemicals
Bacterial Proteins
Heat-Shock Proteins
Recombinant Fusion Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Morrison R P
Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, Montana 59840.
Su H
Lyng K
Yuan Y
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