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- Title
Binding Specificity of Philyra pisum Lectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure.
- Authors
Byung Tae Park; Byung Sun Kim; Heajin Park; Jaehoon Jeong; Hanbit Hyun; Hye Seong Hwang; Ha Hyung Kim
- Abstract
We recently reported a Philyra pisum lectin (PPL) that exerts mitogenic effects on human lymphocytes, and its molecular characterization. The present study provides a more detailed characterization 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, lipopolysaccharide 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.
- Subjects
LYMPHOCYTES; DEGLYCOSYLATION; LECTINS; CELLULAR signal transduction; CRABS; GRAM-positive bacteria
- Publication
Korean Journal of Physiology & Pharmacology, 2013, Vol 17, Issue 6, p547
- ISSN
1226-4512
- Publication type
Article
- DOI
10.4196/kjpp.2013.17.6.547