The Complement Binding and Inhibitory Protein CbiA of Borrelia miyamotoi Degrades Extracellular Matrix Components by Interacting with Plasmin(ogen).

作者: Ngoc T. T. Nguyen , Florian Röttgerding , Gayatri Devraj , Yi-Pin Lin , Arno Koenigs

DOI: 10.3389/FCIMB.2018.00023

关键词:

摘要: The emerging relapsing fever spirochete Borrelia (B.) miyamotoi is transmitted by ixodid ticks and causes the so-called hard tick-borne or B. disease (BMD). More recently, we identified a surface-exposed molecule, CbiA exhibiting complement binding inhibitory capacity rendering spirochetes resistant to complement-mediated lysis. To gain deeper insight into molecular principles of miyamotoi-host interaction, examined as plasmin(ogen) receptor that enables interact with serine protease plasmin(ogen). Recombinant was able bind plasminogen in dose-dependent fashion. Moreover, lysine residues appear play crucial role protein-protein interaction inhibited analog tranexamic acid well increasing ionic strength. Of relevance, bound can be converted urokinase-type activator (uPa) active plasmin which cleaved both, chromogenic substrate S-2251 its physiologic fibrinogen. Concerning involvement specific amino acids plasminogen, located at C-terminus are frequently involved reported for various other plasminogen-interacting proteins Lyme spirochetes. Lysine within C-terminal domain were substituted alanine generate single, double, triple, quadruple point mutants. However, mutated not affected, suggesting distant from might interaction.

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