Tateno Hiroaki, Ogawa Tomohisa, Muramoto Koji, Kamiya Hisao, Saneyoshi Mineo
Department of Biological Resource Sciences, Graduate School of Agricultural Science, Tohoku University, Sendai, Japan.
Biosci Biotechnol Biochem. 2002 Mar;66(3):604-12. doi: 10.1271/bbb.66.604.
The interaction between bacteria and three L-rham-nose-binding lectins, named STL1, STL2, and STL3, from steelhead trout (Oncorhynchus mykiss) eggs was investigated. Although STLs bound to most Gram-negative and Gram-positive bacteria, they agglutinated only Escherichia coli K-12 and Bacillus subtilis among the bacteria tested. The binding was inhibited by L-rhamnose. STLs bound to distinct serotypes of lipopolysaccharides (LPSs), and showed much higher binding activities to smooth-type LPSs of Escherichia coli K-12 and Shigella flexneri 1A than to their corresponding rough-type LPSs. STLs also bound to lipoteichoic acid (LTA) of Bacillus subtilis. These results indicate that STLs bound to bacteria by recognizing LPSs or LTA on the cell surfaces.