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Christopher Lohans
 Christopher Lohans
Assistant Professor
Contact Info
Botterell Hall, Room 615

Academic Background

  • 2015 – 2019 – Post-Doctoral Research Associate (Christopher Schofield), Department of Chemistry, University of Oxford
  • 2009 – 2014 – Ph.D. in Organic Chemistry (John Vederas), Department of Chemistry, University of Alberta
  • 2005 – 2009 – B.Sc. in Chemistry, Department of Chemistry and Biochemistry, University of Regina

Research Interests

Our lab uses methods from biochemistry, chemistry, and microbiology to study antimicrobial resistance. We focus on the beta-lactam antibiotics (e.g., penicillins, carbapenems), looking at their interactions with bacterial beta-lactamases and transpeptidases. We are interested in understanding the mechanisms by which these enzymes degrade beta-lactam antibiotics and beta-lactamase inhibitors, and how they may evolve to overcome new generations of antibiotics and inhibitors.

Interested students are encouraged to get in touch regarding research opportunities.

Visit our lab website at for more information.

Selected Publications

  1. Lohans, C.T.,* Freeman, E.I., van Groesen, E., Tooke, C.L., Hinchliffe, P., Spencer, J., Brem, J., and Schofield, C.J.* Mechanistic insights into β-lactamase-catalysed carbapenem degradation through product characterisation. Sci. Rep. accepted. *co-corresponding
  2. van Groesen, E.,# Lohans, C.T.,#* Brem, J.,# Aertker, K.M.J., Claridge, T.D.W., and Schofield, C.J.* 19F NMR monitoring of reversible protein post-translational modifications: class D β-lactamase carbamylation and inhibition. Chem. Eur. J. accepted (doi:10.1002/chem.201902529). #equal contributions *co-corresponding
  3. de Munnik, M., Lohans, C.T.,* Langley, G.W., Bon, C., Brem, J., and Schofield, C.J.* A fluorescence-based assay for screening β-lactams targeting the Mycobacterium tuberculosis transpeptidase LdtMt2. ChemBioChem accepted (doi:10.1002/cbic.201900379). *co-corresponding
  4. de Munnik, M., Lohans, C.T., Lang, P.A., Langley, G.W., Malla, T.R., Tumber, A., Schofield, C.J.,* and Brem, J.* Targeting the Mycobacterium tuberculosis transpeptidase LdtMt2 with cysteine-reactive inhibitors including ebselen. Chem. Commun. accepted (doi:10.1039/C9CC04145A). Featured on journal cover. *co-corresponding
  5. Lohans, C.T.,# Chan, H.T.H.,# Malla, T., Kumar, K., Kamps, J.J.A.G., McArdle, D.J.B., van Groesen, E., de Munnik, M., Tooke, C.L., Spencer, J., Paton, R.S., Brem, J., and Schofield, C.J. Non-hydrolytic β-lactam antibiotic fragmentation by L,D-transpeptidases and serine β-lactamase cysteine variants. Angew. Chem. Int. Ed. 58, 1990-1994 (2019). #equal contributions
  6. Lohans, C.T., van Groesen, E., Kumar, K., Tooke, C.L., Spencer, J., Paton, R.S., Brem, J., and Schofield, C.J. A new mechanism for β-lactamases: class D enzymes degrade 1β-methyl carbapenems through lactone formation. Angew. Chem. Int. Ed. 130, 1296-1299 (2018).
  7. Rabe, P.,# Kamps, J.J.A.G.,# Schofield, C.J.,#* and Lohans, C.T.#* Roles of 2-oxoglutarate oxygenases and isopenicillin N synthase in β-lactam biosynthesis. Nat. Prod. Rep. 35, 735-756 (2018). Featured on journal cover. #equal contributions *co-corresponding
  8. Lohans, C.T., Brem, J., and Schofield, C.J. New Delhi metallo-b-lactamase-1 catalyses avibactam and aztreonam hydrolysis. Antimicrob. Agents Chemother. 61, e01224-17 (2017) (doi: 10.1128/AAC.01224-17).
  9. Lohans, C.T., Wang, D.Y., Jorgensen, C., Cahill, S.T., Clifton, I.J., McDonough, M.A., Oswin, H.P., Spencer, J., Domene, C., Claridge, T.D.W., Brem, J., and Schofield, C.J. 13C-Carbamylation as a mechanistic probe for the inhibition of class D b-lactamases by avibactam and halide ions. Org. Biomol. Chem. 15, 6024-6032 (2017).
  10. Cahill, S.T., Cain, R., Wang, D.Y., Lohans, C.T., Wareham, D.W., Oswin, H.P., Mohammed, J., Spencer, J., Fishwick, C.W.G., McDonough, M.A., Schofield, C.J., and Brem, J. Cyclic boronates inhibit all classes of b-lactamase. Antimicrob. Agents Chemother. 61, e02260-16 (2017) (doi:10.1128/AAC.02260-16).
  11. Lohans, C.T.,# Wang, D.Y.,# Wang, J., Hamed, R.B., and Schofield, C.J. Crotonases: nature’s exceedingly convertible catalysts. ACS Catal. 7, 6587-6599 (2017). #equal contributions
  12. Cochrane, S.A.,# Lohans, C.T.,# van Belkum, M.J.,# Bels, M.A., and Vederas, J.C. Studies on tridecaptin B1, a new tridecaptin analogue with activity against multidrug resistant Gram-negative bacteria. Org. Biomol. Chem. 13, 6073-6081 (2015). #equal contributions
  13. Lohans, C.T., Li, J.L., and Vederas, J.C. Structure and biosynthesis of carnolysin, a homologue of enterococcal cytolysin with D-amino acids. J. Am. Chem. Soc. 136, 13150-13153 (2014).
  14. Cochrane, S.A., Lohans, C.T., Brandelli, J.R., Mulvey, G., Armstrong, G.D., and Vederas, J.C. Synthesis and structure-activity relationship studies of N-terminal analogues of the antimicrobial peptide tridecaptin A1. J. Med. Chem. 57, 1127-1131 (2014).
  15. Lohans, C.T., and Vederas, J.C. Structural characterization of thioether-bridged bacteriocins. J. Antibiot. 67, 23-30 (2014).
  16. Tulini, F.L., Lohans, C.T., Bordon, K.C., Zheng, J., Arantes, E.C., Vederas, J.C., and De Martinis, E.C. Purification and characterization of antimicrobial peptides from fish isolate Carnobacterium maltaromaticum C2: carnobacteriocin X and carnolysins A1 and A2. Int. J. Food Microbiol. 173, 81-88 (2014).
  17. Lohans, C.T., van Belkum, M.J., Cochrane, S.A., Huang, Z., Sit, C.S., McMullen, L.M., and Vederas, J.C. Biochemical, structural, and genetic characterization of tridecaptin A1, an antagonist of Campylobacter jejuni. ChemBioChem 15, 243-249 (2014).
  18. Lohans, C.T.,# Towle, K.M.,# Miskolzie, M., McKay, R.T., van Belkum, M.J., McMullen, L.M., and Vederas, J.C. Solution structures of the linear leaderless bacteriocins enterocin 7A and 7B resemble carnocyclin A, a circular antimicrobial peptide. Biochemistry 52, 3987-3994 (2013). #equal contributions
  19. Lohans, C.T., Huang, Z., van Belkum, M.J., Giroud, M., Sit, C.S., Steels, E.M., Zheng, J., Whittal, R.M., McMullen, L.M., and Vederas, J.C. Structural characterization of the highly cyclized lantibiotic paenicidin A via a partial desulfurization/reduction strategy. J. Am. Chem. Soc. 134, 19540-19543 (2012).