Panel Discussion

Domyoung Kim ^a, Seok-Joon Kwon^a, Inseon Lee ^b, Jahyun Nam ^b, Jungbae Kim ^b, and Jonathan S Dordick ^a,*

^a Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY 12180, USA.

^b Department of Chemical and Biological Engineering, Korea University, 145 Anam-ro, Seongbuk-gu, Seoul 02841, Republic of Korea.

ABSTRACT

  Selective elimination of bacterial pathogens from commensal microbial communities is critical to reduce antibiotic resistance and strengthen the human immune system. To avoid elimination of “healthy” bacteria, and thus not perturb the microbiome, it is critical to kill only pathogenic bacteria from the complex microbial consortia. The cell wall binding domains (CBDs) of endo- or bacteriolysins can bind with great avidity to numerous binding sites on the cell surface and have exceptional binding specificity against target bacterial pathogens. We developed the new method for the delivery of antimicrobial AgNPs to target pathogenic bacteria using CBDs. To establish the method, C-terminal AgNP binding peptide (AgNPBP) was fused Avi-tagged EGFP to construct Avi-EGFP-AgNPBP. Both Avi-EGFP-AgNPBP and Avi-EGFP-CBD were expressed in E. coli, and simultaneously in vivo biotinylated to produce biotin-EGFP-AgNPBP and biotin-CBD respectively. These EGFP fusion proteins were self-assembled with streptavidin (SA) to construct the CBD-SA-EGFP-AgNPBP complex that can be bound to AgNPs, resulting in synthesizing CBD-SA-EGFP-AgNPs. The CBD-SA-EGFP-AgNPs could be localized on the cell walls of target pathogenic bacteria and kill the target bacteria more efficiently when compared to the bare AgNPs.