Agglutination of a mulberry pathogenic bacterium, P. syringae pv mori by a mulberry leaf lectin
1998
Sunanta Ratanapo | Montri Chulavatnatol (Kasetsart Univ., Bangkok (Thailand). Faculty of Science. Dept. of Biochemistry)
Two sialic acid specific lectins, MLL1 and MLL2 were purified from leaves of mulberry (Morus alba) by affinity chromatography using GalNAc-agarose column, gel filtration on Sephacryl S-200 and anion-exchange chromatography on DEAE-Sephacel. Tests were carried out to see if they could induce agglutination of P. syringae pv mori, a mulberry pathogenic bacterium causing bacterial blight disease was investigated through the bacterial growth. It was found that only MLL1 but not MLL2 could induce the agglutination of the bacteria during log phase of the growth (8-11 hr). No agglutination of other plant pathogenic and human-pathogenic bacteria tested by MLL1 was found. Among several lectins tested, MLL1 was found to be the most effective. The carbohydrate binding specificity of the MLL1-induced agglutination was determined by a sugar-inhibition test. It was found that N-glycolylneuraminic acid and N-acetylgalactosamine at 12.5 mM and galactose at 25 mM were inhibitory. Bovine submaxillary mucin was the most effective inhibitory glycoprotein. It was 250 times more effective than alpha1-acid glycoprotein and 500 times more effective than fetuin and thyroglobulin. The data suggested a possible role of MLL1 in defense against the mulberry pathogenic bacterium. (Supplemented by NSTDA and KURDI supported to S.R.).
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