scholarly journals The Borrelia burgdorferi outer-surface protein ErpX binds mammalian laminin

Microbiology ◽  
2009 ◽  
Vol 155 (3) ◽  
pp. 863-872 ◽  
Author(s):  
Catherine A. Brissette ◽  
Ashutosh Verma ◽  
Amy Bowman ◽  
Anne E. Cooley ◽  
Brian Stevenson
Keyword(s):  
Extracellular Matrix ◽  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Surface Protein ◽  
Extracellular Matrix Component ◽  
Connective Tissues ◽  
Matrix Component ◽  
Laminin Binding Protein ◽  
Persistently Infect ◽  
Laminin Binding

The Lyme disease spirochaete, Borrelia burgdorferi, can invade and persistently infect its hosts' connective tissues. We now demonstrate that B. burgdorferi adheres to the extracellular matrix component laminin. The surface-exposed outer-membrane protein ErpX was identified as having affinity for laminin, and is the first laminin-binding protein to be identified in a Lyme disease spirochaete. The adhesive domain of ErpX was shown to be contained within a small, unstructured hydrophilic segment at the protein's centre. The sequence of that domain is distinct from any previously identified bacterial laminin adhesin, suggesting a unique mode of laminin binding.

scholarly journals Borrelia burgdorferi BmpA Is a Laminin-Binding Protein

2009 ◽  
Vol 77 (11) ◽  
pp. 4940-4946 ◽  
Author(s):  
Ashutosh Verma ◽  
Catherine A. Brissette ◽  
Amy Bowman ◽  
Brian Stevenson
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Surface Protein ◽  
Human Infection ◽  
Type I ◽  
Binding Domains ◽  
Type Iv ◽  
Extracellular Matrix Components ◽  
Carboxy Terminal ◽  
Laminin Binding

ABSTRACT The Borrelia burgdorferi BmpA outer surface protein plays a significant role in mammalian infection by the Lyme disease spirochete and is an important antigen for the serodiagnosis of human infection. B. burgdorferi adheres to host extracellular matrix components, including laminin. The results of our studies indicate that BmpA and its three paralogous proteins, BmpB, BmpC, and BmpD, all bind to mammalian laminin. BmpA did not bind mammalian type I or type IV collagens or fibronectin. BmpA-directed antibodies significantly inhibited the adherence of live B. burgdorferi to laminin. The laminin-binding domain of BmpA was mapped to the carboxy-terminal 80 amino acids. Solubilized collagen inhibited BmpA-laminin binding, suggesting interactions through the collagen-binding domains of laminin. These results, together with previous data, indicate that BmpA and its paralogs are targets for the development of preventative and curative therapies for Lyme disease.

scholarly journals Hyperglycaemia and aberrated insulin signalling stimulate tumour progression via induction of the extracellular matrix component hyaluronan

2017 ◽  
Vol 141 (4) ◽  
pp. 791-804 ◽  
Author(s):  
Sören Twarock ◽  
Christina Reichert ◽  
Ulrike Peters ◽  
Daniel J. Gorski ◽  
Katharina Röck ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Insulin Signalling ◽  
Tumour Progression ◽  
Extracellular Matrix Component ◽  
Matrix Component

scholarly journals Borrelia burgdorferi Complement Regulator-Acquiring Surface Protein 1 of the Lyme Disease Spirochetes Is Expressed in Humans and Induces Antibody Responses Restricted to Nondenatured Structural Determinants

2006 ◽  
Vol 74 (12) ◽  
pp. 7024-7028 ◽  
Author(s):  
Evelyn Rossmann ◽  
Veronique Kitiratschky ◽  
Heidelore Hofmann ◽  
Peter Kraiczy ◽  
Markus M. Simon ◽  
...  
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Surface Protein ◽  
Factor H ◽  
Antibody Responses ◽  
Dominant Factor ◽  
Serum Samples ◽  
Structural Determinants ◽  
Pathogen Persistence ◽  
Complement Regulator

ABSTRACT Borrelia burgdorferi complement regulator-acquiring surface protein 1 (CRASP-1), the dominant factor H and FHL-1-binding protein of the Lyme disease spirochete B. burgdorferi, is implicated in pathogen persistence and was recently reported to be nonimmunogenic in humans. Here we show that serum samples from Lyme disease patients contain antibodies with exclusive specificity for nondenatured structural determinants of CRASP-1.

The impact of age on cardiac function and extracellular matrix component expression in adverse post-infarction remodeling in mice

2019 ◽  
Vol 119 ◽  
pp. 193-202 ◽  
Author(s):  
Felix Nagel ◽  
David Santer ◽  
Stefan Stojkovic ◽  
Christoph Kaun ◽  
Anne-Kristin Schaefer ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cardiac Function ◽  
Extracellular Matrix Component ◽  
Matrix Component ◽  
The Impact

scholarly journals Borrelia burgdorferi RevA Antigen Binds Host Fibronectin

2009 ◽  
Vol 77 (7) ◽  
pp. 2802-2812 ◽  
Author(s):  
Catherine A. Brissette ◽  
Tomasz Bykowski ◽  
Anne E. Cooley ◽  
Amy Bowman ◽  
Brian Stevenson
Keyword(s):  
Lyme Disease ◽  
Borrelia Burgdorferi ◽  
Surface Protein ◽  
Site Directed Mutagenesis ◽  
Heparin Binding ◽  
Amino Terminal ◽  
Ligand Interactions ◽  
Fibronectin Binding Protein ◽  
Vertebrate Hosts ◽  
Mammalian Infection

ABSTRACT Borrelia burgdorferi, the Lyme disease-causing spirochete, can persistently infect its vertebrate hosts for years. B. burgdorferi is often found associated with host connective tissue, where it interacts with components of the extracellular matrix, including fibronectin. Some years ago, a borrelial surface protein, named BBK32, was identified as a fibronectin-binding protein. However, B. burgdorferi BBK32 mutants are still able to bind fibronectin, indicating that the spirochete possesses additional mechanisms for adherence to fibronectin. We now demonstrate that RevA, an unrelated B. burgdorferi outer surface protein, binds mammalian fibronectin in a saturable manner. Site-directed mutagenesis studies identified the amino terminus of the RevA protein as being required for adhesion to fibronectin. RevA bound to the amino-terminal region of fibronectin. RevA binding to fibronectin was not inhibited by salt or heparin, suggesting that adhesin-ligand interactions are primarily nonionic and occur through the non-heparin-binding regions of the fibronectin amino-terminal domains. revA genes are widely distributed among Lyme disease spirochetes, and the present studies determined that all RevA alleles tested bound fibronectin. In addition, RevB, a paralogous protein found in a subset of B. burgdorferi strains, also bound fibronectin. We also confirmed that RevA is produced during mammalian infection but not during colonization of vector ticks and determined that revA transcription is controlled through a mechanism distinct from that of BBK32.

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