Abstract
Rice chitin elicitor binding protein (CEBiP) is a plasma-membrane glycoprotein with LysM domains. CEBiP shows high-affinity for chitin elicitor and functions as a biological receptor for this elicitor. However the detailed analysis of the structure-activity relationship of CEBiP has not been accomplished. We noticed that tobacco BY-2 cell line lacks chitin elicitor responsiveness as well as CEBiP-like binding proteins in the plasma membrane, which makes the cell line as an excellent system for the heterologous expression of CEBiP-like molecules. Actually, the CEBiP protein expressed in the BY-2 cells showed binding characteristics identical to those of rice CEBiP. These results suggest that the expression system and affinity cross-linking assay are useful for the analysis of CEBiP and also various chitin receptor candidates. Binding characteristics of LysM domain deletion mutants of CEBiP expressed in BY-2 cells are in progress.
