Binding Specificity of Philyra pisum Lectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure.
10.4196/kjpp.2013.17.6.547
- Author:
Byung Tae PARK
1
;
Byung Sun KIM
;
Heajin PARK
;
Jaehoon JEONG
;
Hanbit HYUN
;
Hye Seong HWANG
;
Ha Hyung KIM
Author Information
1. Physical Pharmacy Laboratory, College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea. hahyung@cau.ac.kr
- Publication Type:Original Article
- Keywords:
Antiproliferative activity;
Deglycosylation;
Lectin;
Pathogen-associated molecular patterns;
Secondary structure
- MeSH:
beta-Glucans;
Breast;
Circular Dichroism;
Fungi;
Glycoproteins;
Gram-Negative Bacteria;
Gram-Positive Bacteria;
Hemagglutination;
Humans;
Immune System;
Lipopolysaccharides;
Lymphocytes;
Mannans;
Polysaccharides;
Sensitivity and Specificity*;
Teichoic Acids;
Urinary Bladder Neoplasms
- From:The Korean Journal of Physiology and Pharmacology
2013;17(6):547-551
- CountryRepublic of Korea
- Language:English
-
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 alpha-helix, beta-sheet, beta-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 beta-1,3-glucan from fungi. PPL binds to lipoteichoic acids and mannan, but not to lipopolysaccharides or beta-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 alpha-helix and beta-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.
