13Jun

New FimV paper published

FimV is one of the most challenging proteins we’ve worked on for many reasons, but it is really important for twitching motility in P. aeruginosa. In a very collaborative project involving microbiology, biochemistry, bioinformatics, and structural biology, PhD candidate Ryan Buensuceso and friends showed that a highly conserved segment of the protein at its C-terminus interacts with FimL, an activator of the enzyme that makes cAMP – a small molecule critical to expression of virulence factors. The same region is also responsible for cAMP-independent functions of FimV, making it a good place to target inhibitors. The crystal structure of this region will help in the design of such drugs. Well done everyone!

You can read the paper here.

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