Literature DB >> 32039448

A mutation map for human glycoside hydrolase genes.

Lars Hansen1, Diab M Husein2, Birthe Gericke2, Torben Hansen3, Oluf Pedersen3, Mitali A Tambe4, Hudson H Freeze4, Hassan Y Naim2, Bernard Henrissat1,5, Hans H Wandall1, Henrik Clausen1, Eric P Bennett1,6.   

Abstract

Glycoside hydrolases (GHs) are found in all domains of life, and at least 87 distinct genes encoding proteins related to GHs are found in the human genome. GHs serve diverse functions from digestion of dietary polysaccharides to breakdown of intracellular oligosaccharides, glycoproteins, proteoglycans and glycolipids. Congenital disorders of GHs (CDGHs) represent more than 30 rare diseases caused by mutations in one of the GH genes. We previously used whole-exome sequencing of a homogenous Danish population of almost 2000 individuals to probe the incidence of deleterious mutations in the human glycosyltransferases (GTs) and developed a mutation map of human GT genes (GlyMAP-I). While deleterious disease-causing mutations in the GT genes were very rare, and in many cases lethal, we predicted deleterious mutations in GH genes to be less rare and less severe given the higher incidence of CDGHs reported worldwide. To probe the incidence of GH mutations, we constructed a mutation map of human GH-related genes (GlyMAP-II) using the Danish WES data, and correlating this with reported disease-causing mutations confirmed the higher prevalence of disease-causing mutations in several GH genes compared to GT genes. We identified 76 novel nonsynonymous single-nucleotide variations (nsSNVs) in 32 GH genes that have not been associated with a CDGH phenotype, and we experimentally validated two novel potentially damaging nsSNVs in the congenital sucrase-isomaltase deficiency gene, SI. Our study provides a global view of human GH genes and disease-causing mutations and serves as a discovery tool for novel damaging nsSNVs in CDGHs.
© The Author(s) 2020. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oup.com.

Entities:  

Keywords:  WES; congenital disorders of glycoside hydrolysis; nsSNV

Year:  2020        PMID: 32039448      PMCID: PMC7372926          DOI: 10.1093/glycob/cwaa010

Source DB:  PubMed          Journal:  Glycobiology        ISSN: 0959-6658            Impact factor:   4.313


  54 in total

1.  A classification of glycosyl hydrolases based on amino acid sequence similarities.

Authors:  B Henrissat
Journal:  Biochem J       Date:  1991-12-01       Impact factor: 3.857

2.  A congenital disorder of deglycosylation: Biochemical characterization of N-glycanase 1 deficiency in patient fibroblasts.

Authors:  Ping He; Jeff E Grotzke; Bobby G Ng; Murat Gunel; Hamed Jafar-Nejad; Peter Cresswell; Gregory M Enns; Hudson H Freeze
Journal:  Glycobiology       Date:  2015-04-21       Impact factor: 4.313

3.  A glycogene mutation map for discovery of diseases of glycosylation.

Authors:  Lars Hansen; Allan Lind-Thomsen; Hiren J Joshi; Nis Borbye Pedersen; Christian Theil Have; Yun Kong; Shengjun Wang; Thomas Sparso; Niels Grarup; Malene Bech Vester-Christensen; Katrine Schjoldager; Hudson H Freeze; Torben Hansen; Oluf Pedersen; Bernard Henrissat; Ulla Mandel; Henrik Clausen; Hans H Wandall; Eric P Bennett
Journal:  Glycobiology       Date:  2014-09-28       Impact factor: 4.313

Review 4.  Versatility of chemically synthesized guide RNAs for CRISPR-Cas9 genome editing.

Authors:  Melissa L Kelley; Žaklina Strezoska; Kaizhang He; Annaleen Vermeulen; Anja van Brabant Smith
Journal:  J Biotechnol       Date:  2016-06-30       Impact factor: 3.307

5.  Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation.

Authors:  Jeff E Grotzke; Qiao Lu; Peter Cresswell
Journal:  Proc Natl Acad Sci U S A       Date:  2013-02-11       Impact factor: 11.205

6.  Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells.

Authors:  Volkan Seyrantepe; Karine Landry; Stéphanie Trudel; Jacob A Hassan; Carlos R Morales; Alexey V Pshezhetsky
Journal:  J Biol Chem       Date:  2004-06-22       Impact factor: 5.157

7.  Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.

Authors:  E Ikonen; M Baumann; K Grön; A C Syvänen; N Enomaa; R Halila; P Aula; L Peltonen
Journal:  EMBO J       Date:  1991-01       Impact factor: 11.598

8.  Predicting the functional effect of amino acid substitutions and indels.

Authors:  Yongwook Choi; Gregory E Sims; Sean Murphy; Jason R Miller; Agnes P Chan
Journal:  PLoS One       Date:  2012-10-08       Impact factor: 3.240

9.  In silico identification of new putative pathogenic variants in the NEU1 sialidase gene affecting enzyme function and subcellular localization.

Authors:  Dario Bonardi; Viola Ravasio; Giuseppe Borsani; Alessandra d'Azzo; Roberto Bresciani; Eugenio Monti; Edoardo Giacopuzzi
Journal:  PLoS One       Date:  2014-08-25       Impact factor: 3.240

10.  Cystinuria caused by mutations in rBAT, a gene involved in the transport of cystine.

Authors:  M J Calonge; P Gasparini; J Chillarón; M Chillón; M Gallucci; F Rousaud; L Zelante; X Testar; B Dallapiccola; F Di Silverio
Journal:  Nat Genet       Date:  1994-04       Impact factor: 38.330

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