Direct binding analysis between C-Type lectins and glycans using immunoglobulin receptor fusion proteins

Miyuki Watanabe, Zakaria Omahdi, Sho Yamasaki

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Citations (Scopus)

Abstract

C-type lectins bind to carbohydrate structures in a Ca2+-dependent manner. Some transmembrane forms of lectins act as innate immune receptors and induce signal transduction pathways in macrophages and dendritic cells (DCs). Expressing these receptors in cells bearing a reporter gene is a useful tool to investigate ligand binding and recognition. However, it cannot be used to quantify the precise affinity of the interaction, and the involvement of other proteins remains a possibility. Direct binding between a receptor and its ligand can be investigated using an immunoglobulin receptor (Ig)-fused soluble protein. This binding can be assessed using enzyme-linked immunosorbent assays and flow cytometry, and the fusion protein may also be used in a glycan array. In this chapter, we explain the generation of Ig fusion proteins and subsequent binding assays using these proteins.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages119-128
Number of pages10
DOIs
Publication statusPublished - 2020
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume2132
ISSN (Print)1064-3745
ISSN (Electronic)1940-6029

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

Fingerprint

Dive into the research topics of 'Direct binding analysis between C-Type lectins and glycans using immunoglobulin receptor fusion proteins'. Together they form a unique fingerprint.

Cite this