Severe Combined Immunodeficiency from a Homozygous DNA Ligase 1 Mutant with Reduced Catalytic Activity but Increased Ligation Fidelity.

8-Oxoguanine LIG1 SCID autosomal recessive homozygous immunophenotyping magnesium molecular dynamic simulations residue interaction network whole exome sequencing

Journal

Journal of clinical immunology
ISSN: 1573-2592
Titre abrégé: J Clin Immunol
Pays: Netherlands
ID NLM: 8102137

Informations de publication

Date de publication:
19 Jun 2024
Historique:
received: 30 04 2024
accepted: 10 06 2024
medline: 19 6 2024
pubmed: 19 6 2024
entrez: 19 6 2024
Statut: epublish

Résumé

A cell's ability to survive and to evade cancer is contingent on its ability to retain genomic integrity, which can be seriously compromised when nucleic acid phosphodiester bonds are disrupted. DNA Ligase 1 (LIG1) plays a key role in genome maintenance by sealing single-stranded nicks that are produced during DNA replication and repair. Autosomal recessive mutations in a limited number of individuals have been previously described for this gene. Here we report a homozygous LIG1 mutation (p.A624T), affecting a universally conserved residue, in a patient presenting with leukopenia, neutropenia, lymphopenia, pan-hypogammaglobulinemia, and diminished in vitro response to mitogen stimulation. Patient fibroblasts expressed normal levels of LIG1 protein but exhibited impaired growth, poor viability, high baseline levels of gamma-H2AX foci, and an enhanced susceptibility to DNA-damaging agents. The mutation reduced LIG1 activity by lowering its affinity for magnesium 2.5-fold. Remarkably, it also increased LIG1 fidelity > 50-fold against 3' end 8-Oxoguanine mismatches, exhibiting a marked reduction in its ability to process such nicks. This is expected to yield increased ss- and dsDNA breaks. Molecular dynamic simulations, and Residue Interaction Network studies, predicted an allosteric effect for this mutation on the protein loops associated with the LIG1 high-fidelity magnesium, as well as on DNA binding within the adenylation domain. These dual alterations of suppressed activity and enhanced fidelity, arising from a single mutation, underscore the mechanistic picture of how a LIG1 defect can lead to severe immunological disease.

Identifiants

pubmed: 38896336
doi: 10.1007/s10875-024-01754-1
pii: 10.1007/s10875-024-01754-1
doi:

Substances chimiques

DNA Ligase ATP EC 6.5.1.1
LIG1 protein, human 0

Types de publication

Journal Article Case Reports

Langues

eng

Sous-ensembles de citation

IM

Pagination

151

Subventions

Organisme : King Abdullah University of Science and Technology
ID : CRG8 URF/1/4036-01-01
Organisme : King Abdullah University of Science and Technology
ID : CRG8 URF/1/4036-01-01

Informations de copyright

© 2024. The Author(s).

Références

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Auteurs

Huda Alajlan (H)

Translational Genomics, Centre for Genomic Medicine, King Faisal Specialist Hospital & Research Centre, MBC 3, P.O. Box 3354, 11211, Riyadh, Saudi Arabia.

Vlad-Stefan Raducanu (VS)

Bioscience Program, Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, 23955, Thuwal, Saudi Arabia.

Yossef Lopez de Los Santos (Y)

Cell Migration and Signaling Laboratory, Bioscience Program, Division of Biological & Environmental Science & Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.

Muhammad Tehseen (M)

Bioscience Program, Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, 23955, Thuwal, Saudi Arabia.

Hibah Alruwaili (H)

Translational Genomics, Centre for Genomic Medicine, King Faisal Specialist Hospital & Research Centre, MBC 3, P.O. Box 3354, 11211, Riyadh, Saudi Arabia.

Amer Al-Mazrou (A)

Cell Therapy and Immunobiology Department, King Faisal Specialist Hospital & Research Centre, Riyadh, Saudi Arabia.

Reem Mohammad (R)

Pediatric Allergy & Immunology, Department of Pediatrics, King Faisal Specialist Hospital & Research Centre, MBC 3, P.O. Box 3354, 11211, Riyadh, Saudi Arabia.

Monther Al-Alwan (M)

Cell Therapy and Immunobiology Department, King Faisal Specialist Hospital & Research Centre, Riyadh, Saudi Arabia.
College of Medicine, Alfaisal University, Riyadh, Saudi Arabia.

Alfredo De Biasio (A)

Bioscience Program, Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, 23955, Thuwal, Saudi Arabia.

Jasmeen S Merzaban (JS)

Cell Migration and Signaling Laboratory, Bioscience Program, Division of Biological & Environmental Science & Engineering (BESE), King Abdullah University of Science and Technology (KAUST), Thuwal, Saudi Arabia.

Hamoud Al-Mousa (H)

Pediatric Allergy & Immunology, Department of Pediatrics, King Faisal Specialist Hospital & Research Centre, MBC 3, P.O. Box 3354, 11211, Riyadh, Saudi Arabia. hamoudalmousa@kfshrc.edu.sa.
College of Medicine, Alfaisal University, Riyadh, Saudi Arabia. hamoudalmousa@kfshrc.edu.sa.

Samir M Hamdan (SM)

Bioscience Program, Division of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, 23955, Thuwal, Saudi Arabia. samir.hamdan@kaust.edu.sa.

Anas M Alazami (AM)

Translational Genomics, Centre for Genomic Medicine, King Faisal Specialist Hospital & Research Centre, MBC 3, P.O. Box 3354, 11211, Riyadh, Saudi Arabia. amalazami@kfshrc.edu.sa.

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