Glycosylation, hypogammaglobulinemia, and resistance to viral infections.

Glycosylation, hypogammaglobulinemia, and resistance to viral infections.

The New England journal of medicine (2014-04-11)

Mohammed A Sadat, Susan Moir, Tae-Wook Chun, Paolo Lusso, Gerardo Kaplan, Lynne Wolfe, Matthew J Memoli, Miao He, Hugo Vega, Leo J Y Kim, Yan Huang, Nadia Hussein, Elma Nievas, Raquel Mitchell, Mary Garofalo, Aaron Louie, Derek C Ireland, Claire Grunes, Raffaello Cimbro, Vyomesh Patel, Genevieve Holzapfel, Daniel Salahuddin, Tyler Bristol, David Adams, Beatriz E Marciano, Madhuri Hegde, Yuxing Li, Katherine R Calvo, Jennifer Stoddard, J Shawn Justement, Jerome Jacques, Debra A Long Priel, Danielle Murray, Peter Sun, Douglas B Kuhns, Cornelius F Boerkoel, John A Chiorini, Giovanni Di Pasquale, Daniela Verthelyi, Sergio D Rosenzweig

PMID24716661

摘要

Genetic defects in MOGS, the gene encoding mannosyl-oligosaccharide glucosidase (the first enzyme in the processing pathway of N-linked oligosaccharide), cause the rare congenital disorder of glycosylation type IIb (CDG-IIb), also known as MOGS-CDG. MOGS is expressed in the endoplasmic reticulum and is involved in the trimming of N-glycans. We evaluated two siblings with CDG-IIb who presented with multiple neurologic complications and a paradoxical immunologic phenotype characterized by severe hypogammaglobulinemia but limited clinical evidence of an infectious diathesis. A shortened immunoglobulin half-life was determined to be the mechanism underlying the hypogammaglobulinemia. Impaired viral replication and cellular entry may explain a decreased susceptibility to infections.