Structural determination of the complement inhibitory domain of Borrelia burgdorferi BBK32 provides insight into classical pathway complement evasion by Lyme disease spirochetes.
The carboxy-terminal domain of the BBK32 protein from Borrelia burgdorferi sensu stricto, termed BBK32-C, binds and inhibits the initiating serine protease of the human classical complement pathway, C1r. In this study we investigated the function of BBK32 orthologues of the Lyme-associated Borrelia...
Main Authors: | Jialei Xie, Hui Zhi, Ryan J Garrigues, Andrew Keightley, Brandon L Garcia, Jon T Skare |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2019-03-01
|
Series: | PLoS Pathogens |
Online Access: | https://doi.org/10.1371/journal.ppat.1007659 |
Similar Items
-
The Classical Complement Pathway Is Required to Control Borrelia burgdorferi Levels During Experimental Infection
by: Hui Zhi, et al.
Published: (2018-05-01) -
Complement Evasion in <i>Borrelia</i> spirochetes: Mechanisms and Opportunities for Intervention
by: Jonathan W. Locke
Published: (2019-06-01) -
Genome stability of Lyme disease spirochetes: comparative genomics of Borrelia burgdorferi plasmids.
by: Sherwood R Casjens, et al.
Published: (2012-01-01) -
The cyclic-di-GMP signaling pathway in the Lyme disease spirochete, Borrelia burgdorferi
by: Elizabeth A. Novak, et al.
Published: (2014-05-01) -
Population bottlenecks during the infectious cycle of the Lyme disease spirochete Borrelia burgdorferi.
by: Ryan O M Rego, et al.
Published: (2014-01-01)