J. T. Skare

This study reports the crystal structure of FbpC and uses molecular dynamics simulations to show conformational dynamics in borrelial C1r inhibitors, revealing structural plasticity in their anti-complement activity.

This study identifies the structural mechanism by which BBK32 inhibits the classical complement pathway by binding and inactivating C1r.

This paper identifies and characterizes ittA, an intergenic sRNA in Borrelia burgdorferi, showing its role in infectivity and tissue tropism through genetic inactivation and transcriptomic/proteomic analyses.