Donnerstag, 9. April 2015

Decorin binding protein

Decorin binding protein

Current study, we show that the expression of decorin-binding protein (Dbp). Structure of decorin binding protein B from Borrelia burgdorferi and its. Decorin binding proteins A and B (DbpA and B) of Borrelia burgdorferi are of critical importance for the virulence of the spirochete.


DbpA - Decorin-binding protein A precursor - Borrelia burgdorferi. Decorin Binding by DbpA and B of Borrelia garinii, Borrelia afzelii. This protein is a component of connective tissue, binds to type I collagen fibrils, and. Conformational Nature of the Borrelia burgdorferi Decorin Binding.


Both Decorin-Binding Proteins A and B Are Critical for the Overall. The Novel Heparin-Binding Motif in Decorin-Binding Protein A from Strain Bof.

Both Decorin-Binding Proteins A and B Are Critical for the Overall

Structure of decorin binding protein B from Borrelia burgdorferi and

Decorin Binding Proteins A and B in the Serodiagnosis of Lyme. The Novel Heparin-Binding Motif in Decorin-Binding Protein A from. GAG portion of decorin is the major binding site of DBPA, although the.


Epitopes That Elicit Protective Antibodies Decorin Binding Protein A. Antibodies to Borrelia-specific proteins have been used to improve. Structure of decorin binding protein B from Borrelia burgdorferi and. Binds to decorin which may mediate the adherence of rgdorferi to collagen fibers in skin and other tissues. Decorin-binding adhesins from Borrelia burgdorferi associated proteoglycan, via two decorin-binding proteins.


Antibodies to recombinant decorin-binding proteins A and B in the. Molecular Analysis of Sequence Heterogeneity among Genes.

Structural mechanisms underlying sequence-dependent variations

Borrelia burgdorferi Explains the Higher Binding Affinity. Antibodies to decorin-binding protein B (DbpB) in the diagnosis of. Both decorin-binding proteins (DbpA and DbpB) of the Lyme disease spirochete Borrelia burgdorferi bind decorin and glycosaminoglycans. Solution Structure of Decorin-Binding Protein A from Borrelia. DbpA and B are expressed during mammalian infection 1 and they.


Decorin-binding Sites for Collagen Type I Are Mainly Located in. (DbpA and DbpB) in the 20kDa molecular weight range. Decorin binds to collagen type I, whereas biglycan in several assay. Assessment of decorin-binding protein A to the infectivity of Borrelia.


Decorin-binding protein A (DBPA ) is an important lipoprotein from the.

DbpA - Decorin-binding protein A precursor - Borrelia burgdorferi

Decorin Binding Proteins of Borrelia burgdorferi Promote Arthritis. Antibodies towards three decorin binding protein B (DbpB) variants were evaluated. The primary structures of these proteins are homologous and can be. Encoding Decorin Binding Proteins A and B of Borrelia burgdorferi Sensu.


Decorin-binding proteins (Dbps) A and B of Borrelia burgdorferi, the agent of Lyme disease, are surface-exposed lipoproteins that presumably bind to the. Decorin - , the free encyclopedia Decorin and biglycan are thought to be the result of a gene duplication. Decorin-binding proteins (Dbp) A and B are well-characterized adhesins of Bbss 14. Affinities of decorin binding protein A, a Borrelia burgdorferi adhesin.


Decorin binding protein A (DbpA) has been shown by several laboratories to be a. Decorin-binding proteins (DBPs DBPA and DBPB, are surface lipoproteins on Borrelia burgdorferi, the causative agent of Lyme disease.

Antibodies to recombinant decorin-binding proteins A and B in the

Suspected neuroborreliosis (SNB) from Finland were analysed for antibodies to decorin-binding proteins A (DbpA) and. Decorin-binding proteins A and B confer distinct mammalian cell. Decorin binding proteins (Dbp) A and B are surface-exposed outer membrane lipoproteins that mediate the attachment of Borrelia to the extracellular matrix and. Antibodies to decorin-binding protein B (DbpB) in the diagnosis of Lyme neuroborreliosis.


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