Team:HZAU-China/Engineering
Engineering
This year, we have summited two new parts to the registry to prove our Engineering Success.
LRAP
LRAP can self-assemble into a chain structure composed of nanospheres by relying on its C-terminal domain, and the presence of calcium ions can enhance its ability. Non-phosphorylated LRAP tends to induce the formation of ordered hydroxyapatite (HA), while phosphorylated LRAP tend to stabilize amorphous calcium phosphate (ACP) and prevent their conversion to HA in vitro. So the non-phosphorylation LRAP are sufficient to transform ACP into ordered bundles of apatite crystals.We also found that LRAP has the ability to bind to natural teeth.
ClyR
This chimeric lysin can bind to S. mutans by a cell-wall binding domain and then lysis its cell wall from outside by a catalytic domain. ClyR has no activity for Gram-negative bacteria and can be expressed in Escherichia coli. With the guidance of appropriate signal peptide, ClyR can be secreted to the outside of the cells, killing S. mutans in the environment.
ClyR fused with PhoA signal peptide
PhoA fused ClyR can be secreted to the outside of the E.coli
