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Epithelial IgG and its relationship to the loss of F508 in the common mutant form of the cystic fibrosis transmembrane conductance regulator
Author(s) -
Treharne Kate J.,
Cassidy Diane,
Goddard Catharine,
Colledge William H.,
Cassidy Andrew,
Mehta Anil
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.07.002
Subject(s) - cystic fibrosis transmembrane conductance regulator , δf508 , cystic fibrosis , mutant , immune system , transmembrane protein , antibody , inflammation , biology , regulator , phenotype , immunology , potentiator , microbiology and biotechnology , chemistry , genetics , gene , receptor
The most debilitating feature of cystic fibrosis (CF) disease is uncontrolled inflammation of respiratory epithelium. The relationship between the commonest mutated form of CFTR (F508del or ΔF508) and inflammation has not yet been elucidated. Here, we present a new paradigm suggesting that CFTR can interact with intra‐epithelial IgG, establishing a direct link between normal CFTR and the immune system. Further, our data show that the amino‐acid sequence local to F508 can bind IgG with high affinity, dependent on F508, such that loss of F508 abolishes this link both in vitro and in the intact cell.