| Literature DB >> 24716661 |
Mohammed A Sadat1, Susan Moir1, Tae-Wook Chun1, Paolo Lusso1, Gerardo Kaplan1, Lynne Wolfe1, Matthew J Memoli1, Miao He1, Hugo Vega1, Leo J Y Kim1, Yan Huang1, Nadia Hussein1, Elma Nievas1, Raquel Mitchell1, Mary Garofalo1, Aaron Louie1, Derek C Ireland1, Claire Grunes1, Raffaello Cimbro1, Vyomesh Patel1, Genevieve Holzapfel1, Daniel Salahuddin1, Tyler Bristol1, David Adams1, Beatriz E Marciano1, Madhuri Hegde1, Yuxing Li1, Katherine R Calvo1, Jennifer Stoddard1, J Shawn Justement1, Jerome Jacques1, Debra A Long Priel1, Danielle Murray1, Peter Sun1, Douglas B Kuhns1, Cornelius F Boerkoel1, John A Chiorini1, Giovanni Di Pasquale1, Daniela Verthelyi1, Sergio D Rosenzweig1.
Abstract
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.Entities:
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Year: 2014 PMID： 24716661 PMCID： PMC4066413 DOI： 10.1056/NEJMoa1302846
Source DB: PubMed Journal: N Engl J Med ISSN： 0028-4793 Impact factor: 91.245