Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0167860
Title: An anti-human lutheran glycoprotein phage antibody inhibits cell migration on laminin-511: Epitope mapping of the antibody
Authors: Enomoto-Okawa Y.
Maeda Y.
Harashima N.
Sugawara Y.
Katagiri F.
Hozumi K.
Hui K.M. 
Nomizu M.
Ito Y.
Kikkawa Y.
Keywords: autoantibody
glycoprotein
laminin 10
lutheran glycoprotein
monoclonal antibody
unclassified drug
blood group Lutheran system
epitope
glycoprotein
monoclonal antibody
peptide library
protein binding
single chain fragment variable antibody
adult
animal tissue
Article
cancer growth
cell migration
clinical article
controlled study
enzyme inhibition
epitope mapping
human
human tissue
limit of quantitation
liver cell carcinoma
male
metastasis
mouse
mutagenesis
nonhuman
pathogenesis
periplasm
protein binding
protein function
protein localization
amino acid sequence
blood group Lutheran system
cell motion
cell surface display
chemistry
drug effects
enzyme linked immunosorbent assay
epitope mapping
immunology
isolation and purification
peptide library
procedures
protein domain
tumor cell line
Amino Acid Sequence
Antibodies, Monoclonal
Cell Line, Tumor
Cell Movement
Cell Surface Display Techniques
Enzyme-Linked Immunosorbent Assay
Epitope Mapping
Epitopes
Glycoproteins
Humans
Lutheran Blood-Group System
Peptide Library
Protein Binding
Protein Interaction Domains and Motifs
Single-Chain Antibodies
Issue Date: 2017
Publisher: Public Library of Science
Citation: Enomoto-Okawa Y., Maeda Y., Harashima N., Sugawara Y., Katagiri F., Hozumi K., Hui K.M., Nomizu M., Ito Y., Kikkawa Y. (2017). An anti-human lutheran glycoprotein phage antibody inhibits cell migration on laminin-511: Epitope mapping of the antibody. PLoS ONE 12 (1) : 167860. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0167860
Abstract: The Lutheran glycoprotein (Lu), also known as basal cell adhesion molecule (B-CAM), is an Ig superfamily (IgSF) transmembrane receptor for laminin ?5. Although Lu is not present in normal hepatocytes, its expression is significantly increased in hepatocellular carcinoma (HCC). In this study, we isolated thirteen phage antibodies to Lu from a phage library of peripheral blood from HCC patients, suggesting that these patients produced autoantibodies against endogenous Lu. To characterize the phage antibodies, we determined the Lu domains they recognize. The extracellular domain of Lu contains five IgSF domains, D1-D2- D3-D4-D5. The epitope of one phage antibody (A7) was localized to the D5 domain. The other phage antibodies recognized the D2 domain, which is also recognized by a function blocking mouse monoclonal antibody. One of the antibodies to D2 (C7) inhibited the binding of Lu to ligand, and it also prevented tumor cell migration on laminin-511 (LM-511). However, the C7 scFv purified from the periplasm fraction of bacteria did not exhibit the inhibitory effects, indicating that the scFv form could not sterically inhibit the binding of Lu to LM-511. We also identified the amino acid residues that form the epitope recognized by the C7 phage antibody. Mutagenesis studies showed that Arg247 is necessary for forming the epitope. The C7 phage antibody and its epitope may be useful for developing drugs to prevent HCC progression and/or metastasis. © 2016 Enomoto-Okawa et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/166029
ISSN: 19326203
DOI: 10.1371/journal.pone.0167860
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