کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2182952 | 1095533 | 2014 | 8 صفحه PDF | دانلود رایگان |
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
Journal: Immunobiology - Volume 219, Issue 11, November 2014, Pages 822–829