Sui-Lam Wong, PhD, University of Calgary

Sui-Lam Wong, PhD
Sui-Lam Wong, PhD

The long-term research goals of the Wong laboratory are to develop Bacillus subtilis, a gram-positive bacterium, as a microbial factory to produce biotechnologically important proteins via secretion and to design/produce interesting proteins in their natural and engineered forms. While the development and improvement of the secretion and surface display systems are in progress, several interesting proteins including single-chain antibodies, bacterial plasminogen activators (blood-clot dissolving agents) and streptavidin are selected to evaluate the effectiveness of this expression system. Certain novel and desirable properties will be introduced into these molecules through genetic and protein engineering.



  1. Wu S-C, Wong S-L. Structure-Guided Design of an Engineered Streptavidin with Reusability to Purify Streptavidin-Binding Peptide Tagged Proteins or Biotinylated Proteins. van Veen HW, ed. PLoS ONE. 2013;8(7):e69530. doi:10.1371/journal.pone.0069530.
  2. Keefe, A. D., Wilson, D. S., Seelig, B. & Szostak, J. W. One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-Tag. Protein Expr.Purif. 23, 440-446 (2001).
  3. Barrette-Ng, I. H., Wu, S. C., Tjia, W. M., Wong, S. L. & Ng, K. K. The structure of the SBP-Tag-streptavidin complex reveals a novel helical scaffold bridging binding pockets on separate subunits. Acta crystallographica. Section D, Biological crystallography 69, 879-887, doi:10.1107/S0907444913002576 (2013).
  4. Wu, S. C., Wang, C., Hansen, D. & Wong, S. L. A simple approach for preparation of affinity matrices: Simultaneous purification and reversible immobilization of a streptavidin mutein to agarose matrix. Sci Rep 7, 42849. doi: 10.1038/srep42849 (2017).