Binding Specificity of Philyra pisum Lectin to Pathogen-Associated Molecular Patterns, and Its Secondary Structure
- Authors
- Park, Byung Tae; Kim, Byung Sun; Park, Heajin; Jeong, Jaehoon; Hyun, Hanbit; Hwang, Hye Seong; Kim, Ha Hyung
- Issue Date
- Dec-2013
- Publisher
- KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY
- Keywords
- Antiproliferative activity; Deglycosylation; Lectin; Pathogen-associated molecular patterns; Secondary structure
- Citation
- KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY, v.17, no.6, pp 547 - 551
- Pages
- 5
- Journal Title
- KOREAN JOURNAL OF PHYSIOLOGY & PHARMACOLOGY
- Volume
- 17
- Number
- 6
- Start Page
- 547
- End Page
- 551
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/14120
- DOI
- 10.4196/kjpp.2013.17.6.547
- ISSN
- 1226-4512
2093-3827
- 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.
- Files in This Item
- There are no files associated with this item.
- Appears in
Collections - College of Pharmacy > School of Pharmacy > 1. Journal Articles
![qrcode](https://api.qrserver.com/v1/create-qr-code/?size=55x55&data=https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/14120)
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.