| First Author | Kawada M | Year | 2008 |
| Journal | Lab Invest | Volume | 88 |
| Issue | 8 | Pages | 883-95 |
| PubMed ID | 18490894 | Mgi Jnum | J:138138 |
| Mgi Id | MGI:3804351 | Doi | 10.1038/labinvest.2008.47 |
| Citation | Kawada M, et al. (2008) Chitinase 3-like-1 enhances bacterial adhesion to colonic epithelial cells through the interaction with bacterial chitin-binding protein. Lab Invest 88(8):883-95 |
| abstractText | Dysregulated host/microbial interactions play a pivotal role in the pathogenesis of inflammatory bowel disease. We previously reported that chitinase 3-like-1 (CHI3L1) enhances bacterial adhesion and invasion on/into colonic epithelial cells (CECs). In this study, we designed to identify the exact mechanism of how CHI3L1 enhances the bacterial adhesion on CECs in vitro. As compared with wild type (WT) of Serratia marcescens, chitin binding protein (CBP) 21 knockout strain of S. marcescens significantly decreased the adhesion to SW480 cells that express CHI3L1 endogenously. A CBP21 fusion protein was produced with CBP21-expressing vector, which was transformed into BL21 strain of Escherichia coli. CBP21 overexpression significantly increased the adhesion, but not invasion, of nonpathogenic E. coli. The adhesion of S. marcescens and CBP21-overexpressing E. coli was inhibited by coculture with chitin, but not with other carbohydrates. After overexpressing CHI3L1 on SW480 cells, the adhesion rate of CBP21-overexpressing E. coli was further increased by approximately twofold. Genetically engineered E. coli with a single mutation of either Thy-54 or Glu-55 position of CBP21 exhibited a decreased binding ability, and the binding was 74% diminished by the combined mutations of three amino acids (Thy-54, Glu-55 and Glu-60) as compared with WT. Inhibition of CHI3L1 by anti-CHI3L1 antibody or CHI3L1-specific short interfering RNA reduced the adhesion of CBP21-overexpressing E. coli to CECs. In conclusion, CHI3L1 is involved in the enhancement of CBP-expressing bacterial adhesion to CECs. CBP21 and its homologs may be required for the CHI3L1-mediated enhancement of bacterial adhesion to CECs through the conserved amino-acid residues. |
