2004
DOI: 10.1128/jb.186.1.51-60.2004
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Analysis of Differences in the Functional Properties of the Substrate Binding Proteins of the Borrelia burgdorferi Oligopeptide Permease ( opp ) Operon

Abstract: The Borrelia burgdorferi genome encodes five orthologues of the substrate binding protein oligopeptide permease A (OppA). It was previously shown that these genes are under the control of separate promoters and are differentially expressed under various environmental conditions. We were interested in determining whether there are also differences in substrate specificities among the proteins. The substrate specificities of recombinant proteins were determined by screening for high-affinity peptides by use of a… Show more

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Cited by 44 publications
(54 citation statements)
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“…However, the observed low-frequency C-terminal cleavage of wild-type OspC may also represent evidence for a quality control mechanism that senses proper translocation of surface lipoproteins by detecting the release of C-terminal peptides, potentially via the oligopeptide peptide permease complexes in the borrelial IM (8,31,50,57). Disruption of such a mechanism may elicit a bacterial envelope stress response, which could be partially responsible for the secondary effects of ctpA deletion observed by Ö stberg et al (38).…”
Section: Resultsmentioning
confidence: 98%
“…However, the observed low-frequency C-terminal cleavage of wild-type OspC may also represent evidence for a quality control mechanism that senses proper translocation of surface lipoproteins by detecting the release of C-terminal peptides, potentially via the oligopeptide peptide permease complexes in the borrelial IM (8,31,50,57). Disruption of such a mechanism may elicit a bacterial envelope stress response, which could be partially responsible for the secondary effects of ctpA deletion observed by Ö stberg et al (38).…”
Section: Resultsmentioning
confidence: 98%
“…However, unlike other bacteria, B. burgdorferi has 5 open reading frames (ORFs) annotated as homologs of OppA, suggesting that these proteins could play a significant role in acquiring select nutrients/solutes in specific microenvironments (11). Three of these OppA homologs (OppA1, -2, and -3) encoded on the chromosome bound heptapeptides with high affinities in a pH-dependent manner, while the other two homologs present on plasmids (OppA4 on cp26 and OppA5 or BBA34 on lp54) did not exhibit such binding characteristics (84,85). Additional studies also indicated that bba34 was upregulated when the culture conditions of B. burgdorferi were shifted from 25°C to 37°C and in spirochetes present in infected mouse tissues (52).…”
mentioning
confidence: 99%
“…Molecular determinants that connect the external environment to the metabolic status of B. burgdorferi that eventually lead to host-specific adaptation are yet to be characterized in detail. Therefore, we focused on bba34 as a probable mediator of transport of key substances that modulate adaptation to vertebrate hosts since it was (i) upregulated under vertebrate host-specific conditions (52); (ii) downregulated in the csrA Bb mutant (41); (iii) similar to other bacterial solute-binding proteins (31); and (iv) incapable of binding peptides, unlike other OppA homologs of B. burgdorferi (84).…”
mentioning
confidence: 99%
“…Besides transporting oligopeptides, the Opp systems in several pathogenic bacteria (Wang et al, 2004;Moutran et al, 2004;Flores-Valdez et al, 2009;Moraes et al, 2014) participate in distinct life processes, including the binding of soluble host proteins (Cundell et al, 1995;Henrich et al, 1999;Fenno et al, 2000), cellular signal transudation (Ruhfel et al, 1993), recycling of cell-wall peptides released from the growing peptidoglycan (Goodell and Higgins, 1987), and initiation of sporulation (Perego et al, 1991). The Opp system plays a leading role in imparting cell sensitivity to aminoglycoside antibiotics (Kashiwagi et al, 1992), and imparts virulence and pathogenicity to the organisms (Moraes et al, 2014).…”
Section: Introductionmentioning
confidence: 99%