Proteomic analysis of Lyme disease: Global protein comparison of three strains ofBorrelia burgdorferi

Jacobs, Jon; Yang, Xiaohua; Luft, Benjamin J.; Dunn, John J.; Camp, David G.; Smith, Richard D.

doi:10.1002/pmic.200401052

Cited by 17 publications

(25 citation statements)

References 35 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To estimate the relative abundance of each identified protein in the sample, the number of peptides observed for each protein in a sample was divided by the total number of peptides (i.e., both macrophage and S. Typhimurium peptides) found in the same sample (37). Similar approaches have been reported previously (3,16,18,19,25,31,43). Only proteins identified by at least three unique peptide observations that met both SEQUEST and Peptide Prophet criteria were reported.…”

Section: Methodsmentioning

confidence: 81%

Proteomic Investigation of the Time Course Responses of RAW 264.7 Macrophages to Infection with Salmonella enterica

et al. 2009

Self Cite

View full text Add to dashboard Cite

To investigate the extent to which macrophages respond to Salmonella infection, we infected RAW 264.7 macrophages with Salmonella enterica serotype Typhimurium and analyzed macrophage proteins at various time points following infection by using a global proteomic approach. A total of 1,006 macrophage and 115 Salmonella proteins were identified with high confidence. Most of the Salmonella proteins were observed in the late stage of the infection time course, which is consistent with the fact that the bacterial cells proliferate inside RAW 264.7 macrophages. The peptide abundances of most of the identified macrophage proteins remained relatively constant over the time course of infection. Compared to those of the control, the peptide abundances of 244 macrophage proteins (i.e., 24% of the total identified macrophage proteins) changed significantly after infection. The functions of these Salmonella-affected macrophage proteins were diverse, including production of antibacterial nitric oxide (i.e., inducible nitric oxide synthase), production of prostaglandin H 2 (i.e., cyclooxygenase 2), and regulation of intracellular traffic (e.g., sorting nexin 5 [SNX5], SNX6, and SNX9). Diverse functions of the Salmonella-affected macrophage proteins demonstrate a global macrophage response to Salmonella infection. Western blot analysis not only confirmed the proteomic results for a selected set of proteins but also revealed that (i) the protein abundance of mitochondrial superoxide dismutase increased following macrophage infection, indicating an infection-induced oxidative stress in mitochondria, and (ii) in contrast to infection of macrophages by wild-type Salmonella, infection by the sopB deletion mutant had no negative impact on the abundance of SNX6, suggesting a role for SopB in regulating the abundance of SNX6.

show abstract

Section: Methodsmentioning

confidence: 81%

Proteomic Investigation of the Time Course Responses of RAW 264.7 Macrophages to Infection with Salmonella enterica

et al. 2009

Self Cite

View full text Add to dashboard Cite

show abstract

“…The number of peptide observations from each protein was used to estimate the relative abundance of the corresponding protein in the sample. Similar approaches have been previously described (Adkins et al, 2002; Gao et al, 2003; Ishihama et al, 2005; Jacobs et al, 2005; Liu et al, 2004; Qian et al, 2005b; VerBerkmoes et al, 2006). An arbitrary value of 1 was supplied for missing data points (i.e., no protein observed in a specific condition).…”

Section: Methodsmentioning

confidence: 86%

Proteome of Salmonella Enterica Serotype Typhimurium Grown in a Low Mg2+/pH Medium

Shi

Ansong

Smallwood

et al. 2009

J Proteomics Bioinform

View full text Add to dashboard Cite

To determine the impact of a low Mg2+/pH defined growth medium (MgM) on the proteome of Salmonella enterica serotype Typhimurium, we cultured S. Typhimurium cells in the medium under two different conditions termed MgM Shock and MgM Dilution and then comparatively analyzed the bacterial cells harvested from these conditions by a global proteomic approach. Proteomic results showed that MgM Shock and MgM Dilution differentially affected the S. Typhimurium proteome. MgM Shock induced a group of proteins whose induction usually occurred at low O2 level, while MgM Dilution induced those related to the type III secretion system (T3SS) of Salmonella Pathogenicity Island 2 (SPI2) and those involved in thiamine or biotin biosynthesis. The metabolic state of the S. Typhimurium cells grown under MgM Shock condition also differed significantly from that under MgM Dilution condition. Western blot analysis not only confirmed the proteomic results, but also showed that the abundances of SPI2-T3SS proteins SsaQ and SseE and biotin biosynthesis proteins BioB and BioD increased after S. Typhimurium infection of RAW 264.7 macrophages. Deletion of the gene encoding BioB reduced the bacterial ability to replicate inside the macrophages, suggesting a biotin-limited environment encountered by S. Typhimurium within RAW 264.7 macrophages.

show abstract

“…The principle environmental conditions of pH and temperature constitute important signals leading to alterations in gene transcription [2], [3], [4], [5], [6], [7], [8], [9], [10], [11] and protein expression [4], [12], [13], [14], [15] thought to facilitate the bacterial transmission process from tick to mammalian host. For example, the temperature and pH environment of the Ixodes tick midgut is altered following a blood meal [3].…”

Section: Introductionmentioning

confidence: 99%

“…Previous mass spectrometry (MS)-based proteomics studies provided a foundation for the current effort in that Jacobs et al, described the detectable protein distribution for three different strains of Borrelia all grown in similar culture conditions that allowed for strain-to-strain comparisons [15]. New advances in MS technologies afford even greater depth of coverage than reported in the earlier study.…”

Section: Introductionmentioning

confidence: 99%

Proteome Analysis of Borrelia burgdorferi Response to Environmental Change

et al. 2010

Self Cite

View full text Add to dashboard Cite

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 1,031 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.

show abstract

Proteomic analysis of Lyme disease: Global protein comparison of three strains ofBorrelia burgdorferi

Cited by 17 publications

References 35 publications

Proteomic Investigation of the Time Course Responses of RAW 264.7 Macrophages to Infection with Salmonella enterica

Proteomic Investigation of the Time Course Responses of RAW 264.7 Macrophages to Infection with Salmonella enterica

Proteome of Salmonella Enterica Serotype Typhimurium Grown in a Low Mg2+/pH Medium

Proteome Analysis of Borrelia burgdorferi Response to Environmental Change

Contact Info

Product

Resources

About