Ehrlichia sennetsu groE operon and antigenic properties of the GroEL homolog

• Published in: FEMS immunology and medical microbiology Vol. 18; no. 1; pp. 39 - 46
• Main Authors: Zhang, Yilan, Ohashi, Norio, Lee, Eunjoo H., Tamura, Akira, Rikihisa, Yasuko
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.05.1997; Blackwell; Oxford University Press
• Subjects: Amino Acid Sequence; Amino acids; Animals; Antigens; Antigens, Bacterial - genetics; Antigens, Bacterial - immunology; Bacteria; Bacterial Proteins - classification; Bacterial Proteins - genetics; Bacterial Proteins - immunology; Bacteriology; Base Sequence; Biological and medical sciences; Cell Line; Chaperonin 60 - classification; Chaperonin 60 - immunology; Chaperonins; Cyanobacteria; Deoxyribonucleic acid; DNA; DNA, Bacterial; Dogs; E coli; Ehrlichia; Ehrlichia - genetics; Ehrlichia - immunology; Ehrlichia sennetsu; Ehrlichiosis; Escherichia coli Proteins; Fundamental and applied biological sciences. Psychology; Gene sequencing; Genetics; groE operon; Heat shock protein; Heat shock proteins; Heat-Shock Proteins - classification; Heat-Shock Proteins - genetics; Heat-Shock Proteins - immunology; Homology; Hsp60 protein; Humans; Immune response; Immune system; Intracellular bacterium; Mice; Microbiology; Molecular Sequence Data; Monoclonal antibodies; Nucleotide sequence; Open reading frames; Operon; Phylogeny; Proteins; Rabbits; Recombinant antigen; rRNA 16S; Sequence analysis; Tumor Cells, Cultured; Intracellular bacterium; operon; Heat shock protein; Recombinant antigen; Ehrlichiaceae; Rickettsiales; Antigenicity; Nucleotide sequence; Operon; DNA; Bacteria; Phylogeny; Recombinant protein; Aminoacid sequence
• ISSN: 0928-8244; 1574-695X; 2049-632X
• DOI: 10.1111/j.1574-695X.1997.tb01025.x

Abstract A clone expressing an immunoreactive 55-kilodalton (kDa) protein of Ehrlichia sennetsu, the causative agent of human Sennetsu ehrlichiosis, was isolated from a gene library of this organism. Sequence analysis of the DNA insert revealed two open reading frames, encoding proteins of 10,620 and 58,225 kDa, respectively. These deduced amino acid sequences were homologous to those of the GroES and GroEL heat shock proteins (HSP) of other bacteria, respectively. Phylogenetic trees based on GroES and GroEL homologs of several bacteria including E. sennetsu showed a relationship similar to that based on 16S rRNA gene sequences. The recombinant and native 55-kDa proteins of E. sennetsu, GroEL homolog, reacted with a monoclonal antibody (SPA807) which recognizes a homologous sequence between human and mycobacterial HSP60 and a polyclonal antibody (SPA804) to cyanobacteria HSP60, but not with antibodies to HSP60 of several other organisms used. Furthermore, anti-recombinant E. sennetsu 55-kDa protein antibody prepared in a rabbit was reactive to HSP60 antigens of other Ehrlichia and Rickettsia species, but not GroEL of E. coli. The recombinant 55-kDa protein would be a useful tool for studying the role of this antigen in the immune response to E. sennetsu infection.