This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Hoffman, P S Articles by Butler, C A Search for Related Content PubMed PubMed Citation Articles by Hoffman, P S Articles by Butler, C A

 Previous Article  |  Next Article 

Infect Immun. 1990 October; 58(10): 3380-3387

Legionella pneumophila htpAB heat shock operon: nucleotide sequence and expression of the 60-kilodalton antigen in L. pneumophila-infected HeLa cells.

Department of Microbiology and Immunology, University of Tennessee, Memphis 38163.

ABSTRACT

A 60-kilodalton (kDa) immunodominant antigen of Legionella pneumophila is a heat shock protein (HSP) of the GroEL class of HSPs. The gene (htpB) coding the 60-kDa protein was localized to a 3.2-kilobase DNA fragment of L. pneumophila cloned into pUC19 (pSH16) (P. S. Hoffman, C. A. Butler, and F. D. Quinn, Infect. Immun. 57:1731-1739, 1989). The nucleotide sequence of the DNA fragment cloned into M13 confirmed two open reading frames, htpA and htpB, that code for proteins of 96 and 548 amino acids, respectively. A consensus heat shock promoter sequence upstream of the start of htpA was identified, and no obvious promoter sequences were detected upstream of htpB. Amino acid sequence comparison studies revealed that the L. pneumophila HtpB protein exhibited 76% homology with the 65-kDa protein of Mycobacterium tuberculosis and 85% homology with both GroEL of Escherichia coli and HtpB of Coxiella burnetii. A comparison of the amino acid sequences among these proteins revealed several regions of nearly absolute sequence conservation, with the variable regions occurring in common areas. The purified L. pneumophila 60-kDa protein was antigenic for human T lymphocytes. Indirect fluorescent antibody studies indicated that the 60-kDa protein may be located in the periplasm or expressed on the surface by intracellular bacteria, suggesting that a stress-related mechanism may be involved in the expression of this immunodominant antigen.

This article has been cited by other articles:

• Edwards, M. T., Fry, N. K., Harrison, T. G. (2008). Clonal population structure of Legionella pneumophila inferred from allelic profiling. Microbiology 154: 852-864 [Abstract] [Full Text]  
• Gaia, V., Fry, N. K., Afshar, B., Luck, P. C., Meugnier, H., Etienne, J., Peduzzi, R., Harrison, T. G. (2005). Consensus Sequence-Based Scheme for Epidemiological Typing of Clinical and Environmental Isolates of Legionella pneumophila. J. Clin. Microbiol. 43: 2047-2052 [Abstract] [Full Text]  
• Gaia, V., Fry, N. K., Harrison, T. G., Peduzzi, R. (2003). Sequence-Based Typing of Legionella pneumophila Serogroup 1 Offers the Potential for True Portability in Legionellosis Outbreak Investigation. J. Clin. Microbiol. 41: 2932-2939 [Abstract] [Full Text]  
• Field, P. R., Santiago, A., Chan, S.-W., Patel, D. B., Dickeson, D., Mitchell, J. L., Devine, P. L., Murphy, A. M. (2002). Evaluation of a Novel Commercial Enzyme-Linked Immunosorbent Assay Detecting Coxiella burnetii-Specific Immunoglobulin G for Q Fever Prevaccination Screening and Diagnosis. J. Clin. Microbiol. 40: 3526-3529 [Abstract] [Full Text]  
• Hennequin, C., Porcheray, F., Waligora-Dupriet, A.-J., Collignon, A., Barc, M.-C., Bourlioux, P., Karjalainen, T. (2001). GroEL (Hsp60) of Clostridium difficile is involved in cell adherence. Microbiology 147: 87-96 [Abstract] [Full Text]  
• Vemulapalli, R., He, Y., Boyle, S. M., Sriranganathan, N., Schurig, G. G. (2000). Brucella abortus Strain RB51 as a Vector for Heterologous Protein Expression and Induction of Specific Th1 Type Immune Responses. Infect. Immun. 68: 3290-3296 [Abstract] [Full Text]  
• Yamaguchi, H., Osaki, T., Kai, M., Taguchi, H., Kamiya, S. (2000). Immune Response against a Cross-Reactive Epitope on the Heat Shock Protein 60 Homologue of Helicobacter pylori. Infect. Immun. 68: 3448-3454 [Abstract] [Full Text]  
• Field, P. R., Mitchell, J. L., Santiago, A., Dickeson, D. J., Chan, S.-W., Ho, D. W. T., Murphy, A. M., Cuzzubbo, A. J., Devine, P. L. (2000). Comparison of a Commercial Enzyme-Linked Immunosorbent Assay with Immunofluorescence and Complement Fixation Tests for Detection of Coxiella burnetii (Q Fever) Immunoglobulin M. J. Clin. Microbiol. 38: 1645-1647 [Abstract] [Full Text]  
• Macellaro, A., Tujulin, E., Hjalmarsson, K., Norlander, L. (1998). Identification of a 71-Kilodalton Surface-Associated Hsp70 Homologue in Coxiella burnetii. Infect. Immun. 66: 5882-5888 [Abstract] [Full Text]  
• Garduno, R. A., Garduno, E., Hoffman, P. S. (1998). Surface-Associated Hsp60 Chaperonin of Legionella pneumophila Mediates Invasion in a HeLa Cell Model. Infect. Immun. 66: 4602-4610 [Abstract] [Full Text]  
• Zhang, Y., Ohashi, N., Rikihisa, Y. (1998). Cloning of the Heat Shock Protein 70 (HSP70) Gene of Ehrlichia sennetsu and Differential Expression of HSP70 and HSP60 mRNA after Temperature Upshift. Infect. Immun. 66: 3106-3112 [Abstract] [Full Text]  
• Qoronfleh, M. W., Bortner, C. A., Schwartzberg, P., Wilkinson, B. J. (1998). Enhanced Levels of Staphylococcus aureus Stress Protein GroEL and DnaK Homologs Early in Infection of Human Epithelial Cells. Infect. Immun. 66: 3024-3027 [Abstract] [Full Text]  
• Frisk, A., Ison, C. A., Lagergard, T. (1998). GroEL Heat Shock Protein of Haemophilus ducreyi: Association with Cell Surface and Capacity To Bind to Eukaryotic Cells. Infect. Immun. 66: 1252-1257 [Abstract] [Full Text]  
• Garduño, R. A., Faulkner, G., Trevors, M. A., Vats, N., Hoffman, P. S. (1998). Immunolocalization of Hsp60 in Legionella pneumophila. J. Bacteriol. 180: 505-513 [Abstract] [Full Text]