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KMID : 0811720130170060547
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Korean Journal of Physiology & Pharmacology
2013 Volume.17 No. 6 p.547 ~ p.552
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Binding Specificity of Philyra pisum Lectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure
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Park Byung-Tae
Kim Byung-Sun
Park Hea-Jin
Jeong Jae-Hoon
Hyun Han-Bit
Hwang Hye-Seong
Kim Ha-Hyung
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Abstract
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We recently reported a Philyra pisum lectin (PPL) that exerts mitogenic effects on human lym-phocytes, and its molecular characterization. The present study provides a more detailed charac-terization of PPL based on the results from a monosaccharide analysis indicating that PPL is a glycoprotein, and circular dichroism spectra revealing its estimated α-helix, β-sheet, β-turn, and random coil contents to be 14.0%, 39.6%, 15.8%, and 30.6%, respectively. These contents are quite similar to those of deglycosylated PPL, indicating that glycans do not affect its intact structure. The binding properties to different pathogen-associated molecular patterns were investigated with hemagglutination inhibition assays using lipoteichoic acid from Gram-positive bacteria, lipopoly-saccharide from Gram-negative bacteria, and both mannan and β-1,3-glucan from fungi. PPL binds to lipoteichoic acids and mannan, but not to lipopolysaccharides or β-1,3-glucan. PPL exerted no significant antiproliferative effects against human breast or bladder cancer cells. These results indicate that PPL is a glycoprotein with a lipoteichoic acid or mannan-binding specificity and which contains low and high proportions of α-helix and β-structures, respectively. These properties are inherent to the innate immune system of P. pisum and indicate that PPL could be involved in signal transmission into Gram-positive bacteria or fungi.
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KEYWORD
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Antiproliferative activity, Deglycosylation, Lectin, Pathogen-associated molecular patterns, Secondary structure
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