Revisiting the CD14: Epitope mapping by Phage Display

Revisiting the CD14: Epitope mapping by Phage Display

Abstract The cluster of differentiation antigen 14 (CD14) is a key molecule of the innate immunity. This pattern recognition receptor binds mainly to lipopolysaccharide (LPS), lipotechoic acid (LTA), arachidonic acid, and thus induces the releases various cytokines, as a defense mechanism. Several s...

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Bibliographic Details
Published in:Immunobiology (1979) Vol. 219; no. 11; pp. 822 - 829
Main Authors: Alves, Patrícia Terra, Fujimura, Patrícia Tiemi, Morais, Léa Duarte da Silva, Goulart, Luiz Ricardo
Format: Journal Article
Language:English
Published: Netherlands Elsevier GmbH 01-11-2014
Subjects:
Advanced Basic Science
Allergy and Immunology
Amino Acid Sequence
Bacteria - immunology
CD14
Cell Surface Display Techniques
Computational Biology
Epitope mapping
Epitope Mapping - methods
Humans
Immunity, Innate
Lipopolysaccharide Receptors - chemistry
Lipopolysaccharide Receptors - immunology
Lipopolysaccharides - immunology
LPS receptor
Models, Molecular
Molecular Mimicry
Molecular Sequence Data
Peptide Library
Peptides - chemistry
Peptides - immunology
Phage Display
Protein Conformation
GPI
PD
Epitope mapping
CD14
lipopolysaccharide
LPS receptor
cluster differentiation 14
glycosilphophatidylinositol
Phage Display
LPS
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Summary:Abstract The cluster of differentiation antigen 14 (CD14) is a key molecule of the innate immunity. This pattern recognition receptor binds mainly to lipopolysaccharide (LPS), lipotechoic acid (LTA), arachidonic acid, and thus induces the releases various cytokines, as a defense mechanism. Several studies suggest that different regions of the amino-terminal portion of the molecule may be involved in the LPS binding; however, controversial results on the recognition sequence still persist. In this work, functional epitopes of the CD14 molecule were mapped through Phage Display by using a 7-mer conformational constrained random peptide library against a monoclonal antibody anti-soluble CD14-fraction ST and a polyclonal anti-CD14. In silico and empirical analyses were performed to map the selected peptides into the CD14 3D structure. Immunoreactivity tests of peptides against bacterial components of Gram+ and Gram− bacteria were performed in order to demonstrate their functional recognition. All peptides strongly reacted against all bacteria, and besides the recognition of the amino-terminal region, we were able to demonstrate a second epitope site in the middle of the receptor. Additional in silico analysis suggests a possible role of CD14 epitopes as natural antimicrobial peptides
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ISSN:0171-2985
1878-3279
DOI:10.1016/j.imbio.2014.07.002