Protection of C3H/He mice from experimental Borrelia burgdorferi infection by immunization with a 110-kilodalton fusion protein

Bey, R.; Larson, Mary E.; Lowery, David E.; Lee, B W; Knutson, K. S.; Simonson, Randy R.; King, Vickie L.

doi:10.1128/iai.63.8.3213-3217.1995

Cited by 9 publications

(2 citation statements)

References 43 publications

(47 reference statements)

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“…These antigens are OspA (5,7,26,29), OspB (8,22), OspC (21,22), and OspF (18). Additionally, a nonsurface fusion protein with a molecular mass of 110 kDa containing a truncated HSP70 (2) has been reported to be protective, and studies have suggested that P39, also known as BmpA, may also be protective (15,25). OspA has been the subject of the most complete studies as an effective protective immunogen in experimental animals (and under evaluation in humans), although some recent data imply that it may have some limitations as a vaccine candidate.…”

mentioning

confidence: 99%

Outer surface protein C (OspC), but not P39, is a protective immunogen against a tick-transmitted Borrelia burgdorferi challenge: evidence for a conformational protective epitope in OspC

et al. 1996

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Outbred mice were immunized with the soluble fraction of a crude Escherichia coli lysate containing either recombinant outer surface protein C (OspC) or P39 of Borrelia burgdorferi B31 (low passage). Following seroconversion, the mice were challenged with an infectious dose of B. burgdorferi B31 via the natural transmission mode of tick bite. Three mice immunized with P39 were not protected; however, all 12 of the recombinant OspC-immunized mice were protected from infection as assayed by culture and serology. Although OspC has been shown to be a protective immunogen against challenge with in vitro-cultured borrelia administered by needle, this study is the first to demonstrate OspC effectiveness against tick-borne spirochetes. Following feeding, all ticks still harbored B. burgdorferi, suggesting that the mechanism of protection is not linked to destruction of the infectious spirochete within the tick. In a separate experiment, groups of four mice were immunized with protein fractions from B. burgdorferi B31 purified by preparative gel electrophoresis in an attempt to identify potential protective antigens. Many of these mice developed high-titer-antibody responses against OspC, but curiously the mice were susceptible to B. burgdorferi infection via tick bite. These results suggest that the protective epitope(s) on OspC is heat sensitive/conformational, a finding which has implications in vaccine development.

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mentioning

confidence: 99%

Outer surface protein C (OspC), but not P39, is a protective immunogen against a tick-transmitted Borrelia burgdorferi challenge: evidence for a conformational protective epitope in OspC

et al. 1996

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“…Although less extensively studied than GroEL, DnaK homologues of many bacterial pathogens have been found to be immunogenic in humans or animals (1,2,5,8,10,47). Furthermore, as has been shown by the experimental infection of mice with Borrelia burgdorferi, immunization with proteins containing DnaK-specific sequences may protect against microbial infection (4).…”

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confidence: 99%

Cloning and Expression of the dnaK Gene of Campylobacter jejuni and Antigenicity of Heat Shock Protein 70

Thiès¹,

Karch

Hartung³

et al. 1999

Infect Immun

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Campylobacter jejuni is a leading cause of infectious diarrhea throughout the world. In addition, there is growing evidence that Guillain-Barré syndrome, an inflammatory demyelinating disease of the peripheral nervous system, is frequently preceded byC. jejuni infection. In the present study, thehrcA-grpE-dnaK gene cluster of C. jejuni was cloned and sequenced. The dnaK gene consists of an open reading frame of 1,869 bp and encodes a protein with a high degree of homology to other bacterial 70-kDa heat shock proteins (HSPs). The overall percentages of identity to the HSP70 proteins ofHelicobacter pylori, Borrelia burgdorferi,Chlamydia trachomatis, and Bacillus subtiliswere calculated to be 78.1, 60.5, 57.2, and 53.8%, respectively. Regions similar to the Escherichia coli ς70promoter consensus sequence and to a cis-acting regulatory element (CIRCE) are located upstream of the hrcA gene. Following heat shock, a rapid increase of dnaK mRNA was detectable, which reached its maximum after 20 to 30 min. A 6-His-tagged recombinant DnaK protein (rCjDnaK-His) was generated inE. coli, after cloning of the dnaK coding region into pET-22b(+), and purified by affinity and gel filtration chromatography. Antibody responses to rCjDnaK-His were significantly elevated, compared to those of healthy individuals, in about one-third of the serum specimens obtained from C. jejuni enteritis patients.

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Identification of Differentially Regulated Edwardsiella ictaluri Proteins During Catfish Serum Treatment

2018

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Edwardsiella ictaluri is a facultative, intracellular, gram-negative bacterium that causes enteric septicemia of catfish (ESC). Edwardsiella ictaluri is known to be resistant to defense mechanisms present in catfish serum, which might aid in its use of a host's bloodstream to become septicemic. However, the precise mechanisms of the survival of E. ictaluri in host serum are not known. Analysis of the response of E. ictaluri to the host serum treatment at a proteomic level might aid in the elucidation of its adaptation mechanisms against defense mechanisms present in catfish serum. Thus, the objective of this study was to identify differentially regulated proteins of E. ictaluri upon exposure to naïve catfish serum. Two-dimensional difference gel electrophoresis (2D-DIGE) followed by in-gel trypsin digestion and MALDI-TOF/TOF analysis were used for identification of differentially expressed E. ictaluri proteins. A total of 19 differentially regulated proteins (7 up- and 12 downregulated) were identified. Among those were four putative immunogenic proteins, two chaperones and eight proteins involved in the translational process, two nucleic acid degradation and integration proteins, two intermediary metabolism proteins, and one iron-ion-binding protein. Further research focusing on the functions of these differentially expressed proteins may reveal their roles in host adaptation by E. ictaluri.

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Protection of C3H/He mice from experimental Borrelia burgdorferi infection by immunization with a 110-kilodalton fusion protein

Cited by 9 publications

References 43 publications

Outer surface protein C (OspC), but not P39, is a protective immunogen against a tick-transmitted Borrelia burgdorferi challenge: evidence for a conformational protective epitope in OspC

Outer surface protein C (OspC), but not P39, is a protective immunogen against a tick-transmitted Borrelia burgdorferi challenge: evidence for a conformational protective epitope in OspC

Cloning and Expression of the dnaK Gene of Campylobacter jejuni and Antigenicity of Heat Shock Protein 70

Identification of Differentially Regulated Edwardsiella ictaluri Proteins During Catfish Serum Treatment

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