Maithili Deshpande

Cache sensor domains of DUF3365/Tll0287 family bind covalent c-type heme through a CXXCH insertion; a signaling member behaves like an NO sensor, a stand-alone one like a redox protein.

The paper identifies a bacterial NO-binding Cache_heme-HAMP receptor that interacts with a Ser/Thr kinase via conserved motifs, revealing a novel mechanism of NO signaling.

The paper develops an ELISA to screen for protein-protein interaction inhibitors, demonstrating its use in blocking lysinoalanine crosslinking in spirochete flagellar hook proteins.

This study identifies two clinically approved small molecules that inhibit lysinoalanine crosslinking in spirochete flagella, reducing bacterial motility and suggesting a new therapeutic approach.