The bacterial Type IV pilus apparatus is a remarkable molecular machine that rapidly assembles and disassembles protein polymers to perform diverse functions related to microbial pathogenesis.
Work in the Craig lab focuses on Type IV pili, hairlike filaments on the surfaces of many bacterial pathogens, such as Vibrio cholerae, pathogenic Escherichia coli and Neisseria spp. Type IV pili are dynamic filaments that rapidly polymerize and depolymerize their pilin subunits in order to perform diverse functions critical to bacterial virulence, including twitching motility, host cell adhesion, microcolony formation, DNA uptake and protein secretion. We are working to understand the process of pilus assembly and disassembly by investigating the molecular architecture of the pilus filaments and their assembly machinery, with the goal of targeting and even exploiting these systems for antimicrobial therapies.
- Gutierrez-Rodarte, M., Kolappan, S., Burrell, B. and Craig, L. (2019) The Vibrio cholerae minor pilin TcpB mediates uptake of the cholera toxin phage CTXf. J Biol Chem, 294, 15698-15710, PMID: 31471320. http://www.jbc.org/content/294/43/15698.full?sid=e9257e27-c932-45d8-9700-1dcc34891b4d
- Craig, L., Forest, K.T. and Maier, B.T. (2019). Type IV pili: dynamics, biophysics and functional consequences. Nat Rev Microbiol 17, PMID: 30988511. https://www.nature.com/articles/s41579-019-0195-4
- Kolappan, S, Ng, D, Yang, G, Harn, T and Craig, L (2015). Crystal Structure of the minor pilin CofB, the initiator of CFA/III pilus assembly in enterotoxigenic Escherichia coli. J. Biol Chem, 290, 25805-25818. http://www.jbc.org/content/290/43/25805.long