Difference between revisions of "Part:BBa K3861001"

Revision as of 20:09, 20 October 2021

rBC2LCN

Burkholderia cenocepacia , a Gram-positive opportunistic bacterial species, possess several virulence factors. Among them are four soluble lectins which are used for host cell recognition and adhesion. One of these lectins is the lectin BC2L. This lectin has been shown to be a “super” lectin, containing two lectin domains, at the C- and N-terminus. These two lectin domains have been shown to have specificity for different substrates and have been proposed to mediate cell adhesion by conjugating with the bacterial membrane and the host's membrane. The N-terminus builds a homotrimer that binds specifically to carbohydrates containing fucose at the interface between monomers.
In 2018 a study by Shimomura et al. (2018) determined that the N-terminus of the BC2L-C lectin could bind to a representative pancreatic cancer cell line (Capan-1) and be used as a delivery system by conjugating it with a drug. It has additionally been shown that this lectin has the potential to recognize other cancer types, such as colorectal cancer, breast cancer and pluripotent stem cells. As a part of our project “TargetTaxi”, we aimed to utilize this lectin for cancer cell recognition and adhesion. The lectin would be exposed at the surface of Salmonella-derived minicells and mediate their binding. The surface display will be mediated by its fusion with a surface display system regulated by AIDA and FimH.

Sequence and Features