Journal article

Partial IFN-γR2 deficiency is due to protein misfolding and can be rescued by inhibitors of glycosylation.

Marcela Moncada-Vélez, Rubén Martinez-Barricarte, Dusan Bogunovic, Xiao-Fei Kong, Lizbeth Blancas-Galicia, Cengiz Tirpan, Guzide Aksu, Quentin B Vincent, Bertrand Boisson, Yuval Itan, Noé Ramírez-Alejo, Satoshi Okada, Alexandra Y Kreins, Vanessa L Bryant, Jose Luis Franco, Mélanie Migaud, Sara Espinosa-Padilla, Marco Yamazaki-Nakashimada, Francisco Espinosa-Rosales, Necil Kutukculer Show all

Blood | Published : 2013


We report a molecular study of the two known patients with autosomal recessive, partial interferon-γ receptor (IFN-γR)2 deficiency (homozygous for mutations R114C and G227R), and three novel, unrelated children, homozygous for S124F (P1) and G141R (P2 and P3). IFN-γR2 levels on the surface of the three latter patients' cells are slightly lower than those on control cells. The patients' cells also display impaired, but not abolished, response to IFN-γ. Moreover, the R114C, S124F, G141R and G227R IFNGR2 hypomorphic alleles all encode misfolded proteins with abnormal N-glycosylation. The mutants are largely retained in the endoplasmic reticulum, although a small proportion reach and function at..

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University of Melbourne Researchers