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 Cluss, R G Articles by Boothby, J T Search for Related Content PubMed PubMed Citation Articles by Cluss, R G Articles by Boothby, J T

 Previous Article  |  Next Article 

Infect Immun. 1990 April; 58(4): 1038-1042

Thermoregulation of protein synthesis in Borrelia burgdorferi.

Department of Biological Sciences, San Jose State University, California 95192.

ABSTRACT

Borrelia burgdorferi, the etiological agent of Lyme disease, infects humans via the bite of a tick. The microbe survives in at least two vastly different environments: an arthropod vector and a warm-blooded host. We examined protein synthesis in B. burgdorferi B31 in response to sudden heat stress, which is similar to that which occurs during the transmission from vector to host. Proteins synthesized after shifts from 28 degrees C to higher temperatures and in pulse-chase experiments were labeled with 3H-labeled amino acids for 4 h and characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. The synthesis of four proteins we designated as heat stress proteins (HSPs) was increased by shifts to higher temperatures (HSP-1, 75 kilodaltons [kDa]; HSP-2, 42 kDa; HSP-3, 39 kDa; and HSP-4, 27 kDa); and the amount of one protein we designated as heat-labile protein 1 (29.5 kDa) was decreased at higher temperatures. At 37 to 40 degrees C, the major heat stress protein, HSP-1, represented 14 to 18% of the total cell protein compared with 1 to 2% of the total cell protein at 28 degrees C. HSP-1 was stable during a 4-h chase at either 40 or 28 degrees C. Demonstration of similar HSPs in low-passage, pathogenic strains of B. burgdorferi suggests that the heat stress response may be common among B. burgdorferi strains and may play a role in Lyme disease.

This article has been cited by other articles:

• Baldridge, G. D., Burkhardt, N. Y., Felsheim, R. F., Kurtti, T. J., Munderloh, U. G. (2008). Plasmids of the pRM/pRF Family Occur in Diverse Rickettsia Species. Appl. Environ. Microbiol. 74: 645-652 [Abstract] [Full Text]  
• Cluss, R. G., Silverman, D. A., Stafford, T. R. (2004). Extracellular Secretion of the Borrelia burgdorferi Oms28 Porin and Bgp, a Glycosaminoglycan Binding Protein. Infect. Immun. 72: 6279-6286 [Abstract] [Full Text]  
• Anderton, J. M., Tokarz, R., Thill, C. D., Kuhlow, C. J., Brooks, C. S., Akins, D. R., Katona, L. I., Benach, J. L. (2004). Whole-Genome DNA Array Analysis of the Response of Borrelia burgdorferi to a Bactericidal Monoclonal Antibody. Infect. Immun. 72: 2035-2044 [Abstract] [Full Text]  
• Concepcion, M. B., Nelson, D. R. (2003). Expression of spoT in Borrelia burgdorferi during Serum Starvation. J. Bacteriol. 185: 444-452 [Abstract] [Full Text]  
• Revel, A. T., Talaat, A. M., Norgard, M. V. (2002). DNA microarray analysis of differential gene expression in Borrelia burgdorferi, the Lyme disease spirochete. Proc. Natl. Acad. Sci. USA 99: 1562-1567 [Abstract] [Full Text]  
• Yang, X., Popova, T. G., Goldberg, M. S., Norgard, M. V. (2001). Influence of Cultivation Media on Genetic Regulatory Patterns in Borrelia burgdorferi. Infect. Immun. 69: 4159-4163 [Abstract] [Full Text]  
• Elias, A. F., Bono, J. L., Carroll, J. A., Stewart, P., Tilly, K., Rosa, P. (2000). Altered Stationary-Phase Response in a Borrelia burgdorferi rpoS Mutant. J. Bacteriol. 182: 2909-2918 [Abstract] [Full Text]  
• Obonyo, M., Munderloh, U. G., Fingerle, V., Wilske, B., Kurtti, T. J. (1999). Borrelia burgdorferi in Tick Cell Culture Modulates Expression of Outer Surface Proteins A and C in Response to Temperature. J. Clin. Microbiol. 37: 2137-2141 [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]