| Literature DB >> 1987088 |
J M Kornak1, C C Kuo, L A Campbell.
Abstract
The antigen-coding region of a 4.2-kb PstI fragment of Chlamydia pneumoniae (pLC3), which encodes a 75-kDa immunoreactive protein recognized during human C. pneumoniae infection, was localized to a 2.0-kb EcoRI fragment. This subclone expressed an immunoreactive fusion protein of ca. 82 kDa. Nucleotide sequence analysis of the C. pneumoniae gene revealed that it consisted of a 1,980-base open reading frame with an inferred 71,550-Da protein of 660 amino acids. Putative Escherichia coli-like promoters and a ribosomal binding site were located in the 5' upstream region, and an 11-base dyad forming a stable stem-loop structure following two in-frame stop codons was identified. The C. pneumoniae 75-kDa protein is a member of the hsp70 family of heat shock proteins and has 87% amino acid similarity with the Chlamydia trachomatis protein.Entities:
Mesh:
Substances:
Year: 1991 PMID: 1987088 PMCID: PMC257820 DOI: 10.1128/iai.59.2.721-725.1991
Source DB: PubMed Journal: Infect Immun ISSN: 0019-9567 Impact factor: 3.441