Nucleotide sequence and analysis of the gene in Borrelia burgdorferi encoding the immunogenic P39 antigen

Simpson, W J

doi:10.1016/0378-1097(94)90444-8

Cited by 34 publications

(64 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…On the basis of their estimated sizes, the 5Ј ends of the cleaved RNA species map to the vicinity of the putative promoter within the 5Ј region of bmpA (43) Table 1). The 5Ј end of the primer-extended products for bmpAB mapped to an A at Ϫ32 (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The corresponding genes are confined to a single locus on the linear chromosome of this organism in the following 5Ј33Ј gene order: bmpD-bmpC-bmpA-bmpB (2,15,33,43). The paralogs share a high degree of homology at both the DNA (56 to 64%) and protein (36 to 46% identity) levels (2,15,33,37,43). Although the function of none of these proteins has been established, the conservation of their genes within the B. burgdorferi sensu lato complex (2,16,33,37,43) and the presence of orthologs in Treponema pallidum (41) and numerous other bacteria (B. burgdorferi genome web site at the Institute for Genomic Research) suggest that these proteins fulfill an essential physiological role.…”

mentioning

confidence: 99%

“…The paralogs share a high degree of homology at both the DNA (56 to 64%) and protein (36 to 46% identity) levels (2,15,33,37,43). Although the function of none of these proteins has been established, the conservation of their genes within the B. burgdorferi sensu lato complex (2,16,33,37,43) and the presence of orthologs in Treponema pallidum (41) and numerous other bacteria (B. burgdorferi genome web site at the Institute for Genomic Research) suggest that these proteins fulfill an essential physiological role.All four paralogs are transcribed in cultured spirochetes (5,11,33,34,35). Whereas the transcription of bmpA, bmpB, and bmpD has been demonstrated by both Northern blotting (33, 34) and reverse transcription (RT-PCR) (11), the very lowlevel expression of bmpC mRNA could be ascertained only by RT-PCR (11).…”

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Expression of thebmpBGene ofBorrelia burgdorferiIs Modulated by Two Distinct Transcription Termination Events

et al. 2005

View full text Add to dashboard Cite

bmp gene family 36 of Borrelia burgdorferi, the agent of Lyme disease, comprises four paralogs: bmpA, bmpB, bmpC, and bmpD. The bmpA and bmpB genes constitute an operon. All four genes have been found to be transcribed in cultured spirochetes. Expression from the bmpAB operon results in three distinct transcripts of 1.1, 1.6, and 2.4 kb, and the relative expression of bmpA mRNA is three-to fourfold greater than that of bmpB mRNA. However, thus far only expression of the BmpA protein has been demonstrated. Therefore, in this study we characterized the origins of the three transcripts and compared the relative expression of the BmpA and BmpB proteins. Northern blotting revealed that the three distinct transcripts originated from a single promoter located upstream of bmpA but terminated either 3 to the bmpA (1.1-kb RNA) or bmpB (2.4-kb RNA) gene or, most unusually, within the bmpB gene (1.6-kb RNA). Termination within the bmpB gene was associated with a functional Rho-independent transcription terminator. At the protein level, we also observed a 4.3-fold greater abundance of BmpA compared to that of BmpB. These studies identify a transcription termination mechanism in B. burgdorferi resulting in the disparate expression of the two genes of the bmpAB operon.Paralogous bmp gene family 36 of Borrelia burgdorferi encodes four putative lipoproteins: BmpA (P39), BmpB, BmpC, and BmpD. The corresponding genes are confined to a single locus on the linear chromosome of this organism in the following 5Ј33Ј gene order: bmpD-bmpC-bmpA-bmpB (2,15,33,43). The paralogs share a high degree of homology at both the DNA (56 to 64%) and protein (36 to 46% identity) levels (2,15,33,37,43). Although the function of none of these proteins has been established, the conservation of their genes within the B. burgdorferi sensu lato complex (2,16,33,37,43) and the presence of orthologs in Treponema pallidum (41) and numerous other bacteria (B. burgdorferi genome web site at the Institute for Genomic Research) suggest that these proteins fulfill an essential physiological role.All four paralogs are transcribed in cultured spirochetes (5,11,33,34,35). Whereas the transcription of bmpA, bmpB, and bmpD has been demonstrated by both Northern blotting (33, 34) and reverse transcription (RT-PCR) (11), the very lowlevel expression of bmpC mRNA could be ascertained only by RT-PCR (11). However, thus far, only the expression of BmpA and BmpD proteins in vitro has been demonstrated (33, 42). The expression of these genes at the RNA level was also examined as a function of culture temperature and pH (11,35). In one study, the expression of bmpC and bmpD was found to decrease by 6-and 2.5-fold, respectively, at 37°C and pH 6.8 compared to the expression level at 23°C and pH 7.5 (35). In a different study, there was no difference in the expression of the four genes in spirochetes cultured at 23, 32, and 37°C (11). The expression of these genes in vivo was recently examined by microarray analysis (21). In mice infected with B. burgdorferi, bmpB, bmpC, and bm...

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Expression of thebmpBGene ofBorrelia burgdorferiIs Modulated by Two Distinct Transcription Termination Events

et al. 2005

View full text Add to dashboard Cite

show abstract

“…From the sequenced borrelial genome, three σ factor homologs were identified: rpoD (σ 70 ), ntrA (σ 54 ), and rpoS (σ S ) (Fraser et al, 1997). Borrelial promoters for genes encoding Osps (Howe et al, 1986;Jianhui et al, 1997), flagellin (Ge et al, 1997), and p39 antigen (Simpson et al, 1994) were identified by their homology to consensus sequences in E. coli. As expected, the predominant σ factor appears to be σ 70 -like.…”

Section: B Organization Of Borrelial Promotersmentioning

confidence: 99%

Characterization of secA-sod operon in Borrellia burgdorferi.

Nichols¹

View full text Add to dashboard Cite

Borrelia burgdorferi, the causative agent of Lyme disease, has been characterized as a microaerophilic spirochete. O2 consumption and utilization potentially yield reactive oxygen intermediates, such as superoxide, hydroxyl radicals, and hydrogen peroxide. This study investigated the expression of the sod gene, which encodes the only, identified oxidative defense mechanism in B. burgdorferi. Using primer extension analysis and RT-PCR, it was found that sod and secA are organized as a single transcriptional unit under the control of σ 70 -like promoter upstream of the secA open reading frame. Generally, gene expression decreases with increased distance from the promoter; however, secA expression was observed to be relatively lower amounts than sod. Both genes were expressed in all phases of growth, with greatest expression observed in stationary phase. Because transcription of most sod genes is tightly regulated by iron concentration, the secA-sod gene expression was analyzed in borrelial cells grown in varying amounts of metal. Ironrestriction did not significantly affect growth nor did it affect transcription of secA or sod.Likewise, no major differences in transcription were observed with restricting or supplementing media with manganese. To test the possibility that the borrelial SOD may function with either iron or manganese as a cofactor as in cambialistic SODs, SOD activity was assayed and the highest activity was observed in increased manganese concentrations.Protein expression profiles of Sh-2-82 cultured in metal-defined media were investigated by one-and two-dimensional gel electrophoresis. Approximately 15 proteins were differentially expressed in response to metal concentration. iv ACKNOWLEDGMENTS

show abstract

Prominent T cell response to a selectivelyin vivo expressedBorrelia burgdorferi outer surface protein (pG) in patients with Lyme disease

Bauer¹,

Hofmann²,

Jahraus³

et al. 2001

Eur. J. Immunol.

View full text Add to dashboard Cite

Diagnosis of Lyme disease by analysis of T cell immune responses in vitro is curtailed by poor correlation between test results and status of infection. This is probably due to the inherent nonspecific activation potential of the causative agent, the spirochete Borrelia burgdorferi, for bystander lymphocytes, in particular via their outer surface lipoproteins. We have now applied a novel protocol to determine specific T cell responses in Lyme disease patients and exclude unrelated cellular responses in vitro. Non‐lipidated spirochetal antigens (OspA, OspC and P39) including those selectively expressed in the mammalian host (pG and BapA) were used for antigenic stimulation and autologous dendritic cells served as antigen‐presenting cells. The majority of patients with well‐defined early and late manifestations of Lyme disease exhibited specific T cell proliferative responses to one or more of the indicated antigens, however at distinct levels. Most notably, among the five antigens tested, pG was specifically recognized by the majority of T cell populations (>70%) – mainly Th1 cells – from patients but not control individuals. These data indicate a causal relationship between B. burgdorferi infection and T cell reactivity to pG, thus making this protein a promising additional diagnostic marker for Lyme disease.

show abstract

Nucleotide sequence and analysis of the gene in Borrelia burgdorferi encoding the immunogenic P39 antigen

Cited by 34 publications

References 23 publications

Expression of thebmpBGene ofBorrelia burgdorferiIs Modulated by Two Distinct Transcription Termination Events

Expression of thebmpBGene ofBorrelia burgdorferiIs Modulated by Two Distinct Transcription Termination Events

Characterization of secA-sod operon in Borrellia burgdorferi.

Prominent T cell response to a selectivelyin vivo expressedBorrelia burgdorferi outer surface protein (pG) in patients with Lyme disease

Contact Info

Product

Resources

About