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Department of Molecular Biology and Biochemistry
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Selected Publications: Craig Lab

  • Craig, L., Forest, K.T. and Maier, B.T. (2019). Type IV pili: dynamics, biophysics and functional consequences. Nat Rev Microbiol 17, PMID: 30988511.
  • 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. 
  • Kolappan, S, Lo,  KY.  Shen, CLJ, Guttman, J.A., and Craig, L. Structure of a conserved Francisella virulence protein FvfA. Acta Cryst D73, 814-821. 

  • Wang, F, Coureuil, M, Osinski, T, Orlova, A, Altindal, T. Gesbert, G, Nassif, X, Egelman, EH* and  Craig, L* (2017) Cryo-electron microscopy reconstruction of the Pseudomonas aeruginosa and Neisseria gonorrhoeae Type IV pili at sub-nanometer resolution. Structure, 25, 1423-1435, PMID 28877506. *Corresponding authors

  • Ng, D, Harn, T, Altindal, T, Kolappan, S, Marles, J.M, Lala, R, Spielman, I, Gao, Y, Hauke, CA Kovacikova, G, Verjee, Z, Taylor, RK, Biais, N* and Craig, L* (2016) The Vibrio cholerae minor pilin TcpB initiates assembly and retraction of the toxin-coregulated pilus. PLoS Pathogens, ePub 10.1371/journal.ppat.1006109, PMID 27992883. *Corresponding authors

  • Ng, D, Harn, T, Altindal, T, Kolappan, S, Marles, JM, Lala, R, Spielman, I, Gao, Y, Hauke, CA Kovacikova, G, Verjee, Z,  Taylor, RK, Biais, N* and Craig, L* (2016). The Vibrio cholerae minor pilin TcpB initiates assembly and retraction of the toxin-coregulated pilus. PLoS Pathogens, ePub 10.1371/journal.ppat.1006109, PMID 27992883. *Corresponding authors

  • Kolappan, S, Coureuil, M Yu, X, Nassif, X, Egelman, EH* and Craig, L* (2016). Structure of the Neisseria meningitidis Type IV pilus. Nat Commun. 7:13015. Doi 10.1038/ncomms13015, PMID 27698424. *Corresponding authors

  • 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. PMID 26324721.

  • Kolappan, S., Shen, D.L., Mosi, R., Sun, J., McEachern, E.J., Vocadlo, D.J. and Craig, L. (2015) Structures of lactate dehydrogenase a (LDHA) in apo-, ternary and inhibitor-bound forms. Acta Cryst. D71, 185-195, 2015. PMID 25664.

  • Yuen, A.S.W., Kolappan, S., Ng, D. and Craig, L. (2013). Structure and secretion of CofJ, a putative colonization factor of enterotoxigenic E. coli. Mol Microbiol, 90, 898-918. PMID 24106767.

  • Kolappan, S. and Craig, L. (2013). Structure of the cytoplasmic domain of TcpE, the inner membrane core protein required for assembly of the Vibrio cholerae toxin coregulated pilus. Acta Cryst D69, 513-519. PMID 23519659.

  • Galkin, V.E.*, Kolappan, S., Ng, D., Zong, Z., Li, J., Egelman, E.H. and Craig, L.* (2013). Structure of the CS1 pilus of enterotoxigenic Escherichia coli reveals structural polymorphism. J Bacteriol, 195,1360-1370. PMID 23175654. *Corresponding authors.

  • Melville, S. & Craig. L. (2013). Type IV pili in Gram-positive bacteria. Microbiol Mol Biol Reviews. 77, 323-341. PMID 24006467.

  • Craig, L. and Taylor, R.K (2013). Vibrio cholerae toxin coregulated pili. In “Bacterial pili: Structure, synthesis and role in disease” for the “Advances in molecular and cellular microbiology” series. Ed. M.A. Barocchi and J.L. Telford, CABI International (CABI Publishing), Wallingford, UK. Chapter 1, 1-16.

  • Ford, C.G., Kolappan, S., Phan, H.T.H., Waldor, M.K., Winther-Larsen, H.C. and Craig, L. (2012). Crystal structures of CTX-phi pIII unbound and in complex with Vibrio cholerae TolA reveal novel interaction interfaces. J Biol Chem, 287, 36258-36272, PMID 22942280.

  • Kolappan, S., Roos, J., Yuen, A., Pierce, O.M., and Craig, L. (2012). Structural characterization of CFA/III and Longus Type IVb pili from enterotoxigenic Escherichia coli. J Bacteriol 194, 2725-2735, PMID 22447901.

  • Yamagata, A., Milgotina, E., Scanlon, K., Craig, L., Tainer, J.A., Donnenberg, M.S. (2012). Structure of an essential Type IV pilus biogenesis protein provides insights into pilus and Type II secretion systems. J Mol Biol 419, 110-124, PMID 22387466.

  • Li, J., Egelman, E.H. and Craig, L. (2012). Structure of the Vibrio cholerae Type IVb pilus and stability comparison with the Neisseria gonorrhoeae Type IVa pilus. J Mol Biol 418, 47-64. PMID 22361030.

  • Kolappan, S., Tracy, E.N., Bakaletz, L.O., Munson, R.S. Jr and Craig, L. (2012). Expression, purification, crystallization and preliminary x-ray diffraction analysis of PilA from the nontypeable Haemophilus influenzae Type IV pilus. Acta Cryst F, F68, 284-287, PMID 22442223.

  • Scott, J.K. Pantophlet, R. and Craig, L. (2012). Molecular grafting of a complex epitope onto a protein scaffold. Commentary in Nature Biotech 30, 154-155, PMID 22318033.

  • Hartung, S., Arvai, A.S., Wood, T., Kolappan, S., Shin, D.S., Craig, L.* and Tainer, J.A.* (2011). Ultra-high resolution and full-length pilin structures with insights for filament assembly, pathogenic functions and vaccine potential. J Biol Chem 286, 44254-44265, PMID 22027840. *Corresponding authors.

  • Megli, C., Yuen, A.S., Kolappan, S., Richardson, M.R. Dharmasena, M.N., Krebs, S.J., Taylor, R.K.* and Craig, L.* (2011). Crystal structure of the Vibrio cholerae colonization factor TcpF and identification of a functional immunogenic site. J. Mol. Biol. 409, 146-158, PMID 21440558. *Corresponding authors.

  • Lim, M.S., Ng, D., Zong, Z., Arvai, A, Taylor, R.K., Tainer, J.A., and Craig, L. (2010). Vibrio cholerae El Tor TcpA crystal structure and mechanism for pilus-mediated microcolony formation. Mol Microbiol 77, 755-770, PMID 20545841.

  • Irving, M.B., Craig L., Menendez, A., Gangadhar, B.P., Montero M., van Houten, N.E. and Scott, J.K. (2010). Exploring peptide mimics for the production of antibodies against discontinuous protein epitopes. Mol Immunol 47, 1137-1148, PMID 20031219.

  • Craig, L. (2009). Type IV pilus structure. In “Pili and flagella: current research and future trends”. Ed. Ken F. Jarrell, Caister Academic Press, Chapter 1, 1-17.

  • Li, J., Lim, M.S., Li, S., Brock, M., Pique, M.E., Woods Jr., V.L. and Craig, L. (2008). Vibrio cholerae toxin-coregulated pilus structure analyzed by hydrogen/deuterium exchange mass spectrometry. Structure, 16, pp. 137-148. PMID 18184591. 

  • Craig, L. and Li., J. (2008). Type IV pili: paradoxes in form and function. Cur Op Struct Biol, 18, 267-277, PMID 18249533.

  • Craig, L., Volkmann N., Arvai A.S., Pique M.E., Yeager M., Egelman E.H, and Tainer J.A. (2006). Type IV pilus structure by cryo-electron microscopy and crystallography: implications for pilus assembly and Functions. Mol Cell 23, 651-662, PMID 16949362.

  • Craig, L., Pique, M.E. and Tainer, J.A. (2004). Type IV pilus structure and bacterial pathogenicity. Nature Rev Microbiol 2, 363-378, PMID 15100690.

  • Shin, D.S., Pellegrini, L., Daniels, D.S., Yelent, B., Craig, L., Bates, D., Yu, D.S., Shivji, M.K., Hitomi, Arvai, A.S., Volkmann, N., Tsuruta, H., Blundell, T.L., Venkitaraman, A.R. and Tainer, J.A. (2003). Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2. EMBO J 22, 4566-4576, PMID 12941707.

  • Didonato, M., Craig, L., Huff, M.E., Thayer, M.M., Cardoso, R.M.F., Kassmann, C.J., Lo, T.P., Koike, C.K., Powers, E.T., Kelly, J.W., Getzoff, E.D. and Tainer, J.A. (2003). ALS mutants of human superoxide dismutase for fibrous aggregates via framework destabilization. J Mol Biol 332, 601-615, PMID 12963370.

  • Craig, L., Taylor, R.K., Pique, M.E., Adair, B.D., Arvai, A.S., Singh, M., Lloyd, S.J., Shin, D.S., Getzoff, E.D., Yeager, M., Forest K.T. and Tainer, J.A. (2003). Type IV pilin structure and assembly: X-ray and EM analyses of Vibrio cholerae toxin-coregulated pilus and Pseudomonas aeruginosa PAK pilin. Mol Cell 11 1139-1150, PMID 12769840.

  • Hopfner, K.P.*, Craig, L.*, Moncalian, G., Zinkel, R.A., Usui, T., Owen, B.A.L., Karcher, A., Henderson, B., Bodmer, J.L., McMurray, C.T., Carney, J.P., Petrini J.H.G. and Tainer, J.A. (2002). Rad50 Zn hook: a novel structure joining Mre11 complexes in DNA recombination and repair. Nature 418, 562-566. PMID 12152085. *These authors contributed equally to this work.

  • Hopfner, K.P., Karcher, A., Craig, L., Woo, T.T., Carney J.P. and Tainer, J.A. (2001). Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50 ATPase. Cell 105, 473-485. PMID 11371344.

  • Hopfner, K.P., Karcher, A., Shin, D.S., Craig, L., Arthur, L.M., Carney J.P. and Tainer, J.A. (2000). Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101: 789-800. PMID 10892749.

  • Craig, L., Sanschagrin, P.C., Rozek, A., Lackie, S., Kuhn, L.A. and Scott, J.K. (1998). The role of structure in antibody cross-reactivity between peptides and folded proteins. J Mol Biol 281, 183-201. PMID 9680484.

  • Harris, S.L., Craig, L., Mehroke, J.S., Rashed, M. Zwick, M.B., Kenar, K., Toone, E.J., Greenspan, N., Auzanneau, F.-I., Marino-Albernas, J.-R., Pinto B.M. and Scott, J.K. (1997). Exploring the basis of peptide-carbohydrate cross-reactivity: evidence for discrimination by peptides between closely related anticarbohydrate antibodies. Proc Natl Acad Sci, USA 94, 2454-2459. PMID 9122216.

  • Craig, L., Johnson J.E. and Cornell, R.B. (1994). Identification of the membrane-binding domain of CTP:phosphocholine cytidylytransferase using chymotrypsin proteolysis. J Biol Chem 269, 3311-3317, PMID 8106370.

  • Scott, J.K. and Craig, L. (1994). Random peptide libraries. Cur Op Biotech. 5, 40-48. PMID 7764642, PMID 7764642.
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