Decorin Binding by DbpA and B of Borrelia garinii, Borrelia afzelii, and Borrelia burgdorferi Sensu Stricto

Salo, Jemiina; Loimaranta, Vuokko; Lahdenne, Pekka; Viljanen, Matti K.; Hytönen, Jukka

doi:10.1093/infdis/jir207

Cited by 30 publications

(37 citation statements)

References 32 publications

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“…These 19-kDa and 20-kDa proteins, respectively, are encoded by and expressed within B. burgdorferi sensu stricto strains and also many B. burgdorferi sensu lato strains, albeit as heterogeneous homologs (12,15,16,17). Expression is upregulated in the mammalian host after tick-borne infection (18), and DbpA and DbpB are highly antigenic during infection (14,19,20).…”

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confidence: 99%

The Early Dissemination Defect Attributed to Disruption of Decorin-Binding Proteins Is Abolished in Chronic Murine Lyme Borreliosis

et al. 2013

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The laboratory mouse model of Lyme disease has revealed that Borrelia burgdorferi differentially expresses numerous outer surface proteins that influence different stages of infection (tick-borne transmission, tissue colonization, dissemination, persistence, and tick acquisition). Deletion of two such outer surface proteins, decorin-binding proteins A and B (DbpA/B), has been documented to decrease infectivity, impede early dissemination, and, possibly, prevent persistence. In this study, DbpA/B-deficient spirochetes were confirmed to exhibit an early dissemination defect in immunocompetent, but not immunodeficient, mice, and the defect was found to resolve with chronicity. Development of disease (arthritis and carditis) was attenuated only in the early stage of infection with DbpA/B-deficient spirochetes in both types of mice. Persistence of the DbpA/B-deficient spirochetes occurred in both immunocompetent and immunodeficient mice in a manner indistinguishable from that of wild-type spirochetes. Dissemination through the lymphatic system was evaluated as an underlying mechanism for the early dissemination defect. At 12 h, 3 days, 7 days, and 14 days postinoculation, DbpA/B-deficient spirochetes were significantly less prevalent and in lower numbers in lymph nodes than wild-type spirochetes. However, in immunodeficient mice, deficiency of DbpA/B did not significantly decrease the prevalence or spirochete numbers in lymph nodes. Complementation of DbpA/B restored a wild-type phenotype. Thus, the results indicated that deficiency of DbpA/B allows the acquired immune response to restrict early dissemination of spirochetes, which appears to be at least partially mediated through the lymphatic system.

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confidence: 99%

The Early Dissemination Defect Attributed to Disruption of Decorin-Binding Proteins Is Abolished in Chronic Murine Lyme Borreliosis

et al. 2013

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“…Tissues contain diversity within their ECM, with various subunits and ratios of collagens, fibronectin, integrins, fibrinogen, and laminin (65). ECM-binding adhesins have been characterized in many pathogens, and some have been discovered in B. burgdorferi, including DbpA, BBK32, P66, Bgp, BBB07, and BBA33 (21)(22)(23)(24)(25)(26)(27)54). B. burgdorferi has an outer surface rich in lipoproteins, many of which are hypothesized to interact with host structures and provide for optimal adhesion and/or immune evasion.…”

Section: Discussionmentioning

confidence: 99%

“…The ability of B. burgdorferi to evade the immune response and colonize tissues lies within the numerous lipoproteins that adorn its outer surface (20). Many of these lipoproteins have been characterized as ECM (extracellular matrix) adhesins, including those that bind to decorin (DbpA), fibronectin (BBK32), glycosaminoglycans (Bgp; BBK32; DbpA), and integrins (BBB07, P66), as well as many others with unknown host ligands (21)(22)(23)(24)(25)(26)(27). B. burgdorferi also expresses on its surface a variable surface antigen, VlsE, and five different factor H binding proteins designated complement regulator-acquiring surface proteins, which are involved in the evasion of complement-dependent killing (28,29).…”

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confidence: 99%

BB0744 Affects Tissue Tropism and Spatial Distribution of Borrelia burgdorferi

et al. 2015

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bBorrelia burgdorferi, the etiologic agent of Lyme disease, produces a variety of proteins that promote survival and colonization in both the Ixodes species vector and various mammalian hosts. We initially identified BB0744 (also known as p83/100) by screening for B. burgdorferi strain B31 proteins that bind to ␣ 1 ␤ 1 integrin and hypothesized that, given the presence of a signal peptide, BB0744 may be a surface-exposed protein. In contrast to this expectation, localization studies suggested that BB0744 resides in the periplasm. Despite its subsurface location, we were interested in testing whether BB0744 is required for borrelial pathogenesis. To this end, a bb0744 deletion was isolated in a B. burgdorferi strain B31 infectious background, complemented, and queried for the role of BB0744 following experimental infection. A combination of bioluminescent imaging, cultivation of infected tissues, and quantitative PCR (qPCR) demonstrated that ⌬bb0744 mutant B. burgdorferi bacteria were attenuated in the ability to colonize heart tissue, as well as skin locations distal to the site of infection. Furthermore, qPCR indicated a significantly reduced spirochetal load in distal skin and joint tissue infected with ⌬bb0744 mutant B. burgdorferi. Complementation with bb0744 restored infectivity, indicating that the defect seen in ⌬bb0744 mutant B. burgdorferi was due to the loss of BB0744. Taken together, these results suggest that BB0744 is necessary for tissue tropism, particularly in heart tissue, alters the ability of B. burgdorferi to disseminate efficiently, or both. Additional studies are warranted to address the mechanism employed by BB0744 that alters the pathogenic potential of B. burgdorferi.

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“…Outside of the streptococcus group of bacteria, decorin binding proteins (Dbp A, DbpB, Bgp) have been described in the spirochete Borrelia burgdorferi sensu lato group (Leong et al, 1998). The decorin binding site of DbpA has been mapped to a conserved peptide motif (EAKVRA), with binding mediated by the GAG chain, particularly DS (Salo et al, 2011). In those studies, DbpA showed considerably stronger binding under the flow conditions provided by SPR analysis, compared with stationary incubation adhesion assays.…”

Section: Discussionmentioning

confidence: 99%

“…In those studies, DbpA showed considerably stronger binding under the flow conditions provided by SPR analysis, compared with stationary incubation adhesion assays. The authors hypothesise that the DbpA adhesion acts as a "catch bond" and sheer force is required to induce stronger interaction with the decorin (Salo et al, 2011).…”

Section: Discussionmentioning

confidence: 99%

Real-time monitoring of the adherence of Streptococcus anginosus group bacteria to extracellular matrix decorin and biglycan proteoglycans in biofilm formation

Landrygan-Bakri¹,

Wilson²,

Williams³

et al. 2012

Research in Microbiology

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Decorin Binding by DbpA and B of Borrelia garinii, Borrelia afzelii, and Borrelia burgdorferi Sensu Stricto

Abstract: Dbp A and B of B. garinii and B. burgdorferi ss mediate the interaction between the spirochete and decorin, whereas the same adhesins of B. afzelii show only negligible activity.

Cited by 30 publications

References 32 publications

The Early Dissemination Defect Attributed to Disruption of Decorin-Binding Proteins Is Abolished in Chronic Murine Lyme Borreliosis

The Early Dissemination Defect Attributed to Disruption of Decorin-Binding Proteins Is Abolished in Chronic Murine Lyme Borreliosis

BB0744 Affects Tissue Tropism and Spatial Distribution of Borrelia burgdorferi

Real-time monitoring of the adherence of Streptococcus anginosus group bacteria to extracellular matrix decorin and biglycan proteoglycans in biofilm formation

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