Proteome Analysis of Borrelia burgdorferi Response to Environmental Change
We examined global changes in protein expression in the B31 strain of Borrelia burgdorferi, in response to two environmental cues (pH and temperature) chosen for their reported similarity to those encountered at different stages of the organism’s life cycle. Multidimensional nano-liquid chromatographic separations coupled with tandem mass spectrometry were used to examine the array of proteins (i.e., the proteome) of B. burgdorferi for different pH and temperature culture conditions. Changes in pH and temperature elicited in vitro adaptations of this spirochete known to cause Lyme disease and led to alterations in protein expression that are associated with increased microbial pathogenesis. We identified 1031 proteins that represent 59% of the annotated genome of B. burgdorferi and elucidated a core proteome of 414 proteins that were present in all environmental conditions investigated. Observed changes in protein abundances indicated varied replicon usage, as well as proteome functional distributions between the in vitro cell culture conditions. Surprisingly, the pH and temperature conditions that mimicked B. burgdorferi residing in the gut of a fed tick showed a marked reduction in protein diversity. Additionally, the results provide us with leading candidates for exploring how B. burgdorferi adapts to and is able to survive in a wide variety of environmental conditions and lay a foundation for planned in situ studies of B. burgdorferi isolated from the tick midgut and infected animals.
- Research Organization:
- Pacific Northwest National Lab. (PNNL), Richland, WA (United States). Environmental Molecular Sciences Lab. (EMSL)
- Sponsoring Organization:
- USDOE
- DOE Contract Number:
- AC05-76RL01830
- OSTI ID:
- 1000107
- Report Number(s):
- PNNL-SA-74148; 24698; 400412000; TRN: US201024%%304
- Journal Information:
- PLoS One, 5(11):Article No.: e13800, Vol. 5, Issue 11
- Country of Publication:
- United States
- Language:
- English
Similar Records
Biochemical and biophysical characterization of the major outer surface protein, OSP-A from North American and European isolates of Borrelia burgdorferi
Genome Stability of Lyme Disease Spirochetes: Comparative Genomics of Borrelia burgdorferi Plasmids
Related Subjects
99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE
ANIMALS
CELL CULTURES
DISEASES
FUNCTIONALS
IN VITRO
LIFE CYCLE
MASS SPECTROSCOPY
PATHOGENESIS
PROTEINS
REPLICONS
STRAINS
TICKS
LYME-DISEASE SPIROCHETE
OUTER SURFACE PROTEIN
HOST-SPECIFIC SIGNALS
GENE-EXPRESSION
MAMMALIAN HOST
INFECTIOUS CYCLE
FACTOR-H
BINDING
TRANSCRIPTOME
REGULATOR
Environmental Molecular Sciences Laboratory