Exome sequencing identifies NFS 1 deficiency in a novel Fe‐S cluster disease, infantile mitochondrial complex II/III deficiency
Open accessAbstract
Iron-sulfur (Fe-S) clusters are a class of highly conserved and ubiquitous prosthetic groups with unique chemical properties that allow the proteins that contain them, Fe-S proteins, to assist in various key biochemical pathways. Mutations in Fe-S proteins often disrupt Fe-S cluster assembly leading to a spectrum of severe disorders such as Friedreich's ataxia or iron-sulfur cluster assembly enzyme (ISCU) myopathy. Herein, we describe infantile mitochondrial complex II/III deficiency, a novel autosomal recessive mitochondrial disease characterized by lactic acidemia, hypotonia, respiratory chain complex II and III deficiency, multisystem organ failure and abnormal mitochondria. Through autozygosity mapping, exome sequencing, in silico analyses, population studies and functional tests, we identified c.215G>A, p.Arg72Gln in NFS1 as the likely causative mutation. We describe the first disease in man likely caused by deficiency in NFS1, a cysteine desulfurase that is implicated in respiratory chain function and iron maintenance by initiating Fe-S cluster biosynthesis. Our results further demonstrate the importance of sufficient NFS1 expression in human physiology.
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Mutations or dysfunctions of Fe-S cluster biogenesis have been linked to multiple inherited disorders such as Friedreich's ataxia, infantile complex II/III deficiency syndrome, and multiple mitochondrial dysfunctions syndromes.
“mutations or dysfunctions of Fe-S cluster biogenesis have been linked to multiple inherited disorders such as Friedreich's ataxia (caused by a disruptive guanine-adenine-adenine repeat in the first intron of FXN) (Campuzano et al., 1996), infantile complex II/III deficiency syndrome (a lethal autosomal recessive disease caused by a point mutation in NFS1) (Farhan et al., 2014) and multiple”
From The Role of Iron Regulation in Immunometabolism and Immune-Related Disease (2019) · cites this paper as Farhan et al., 2014
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Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575503
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575497
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575554
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575524
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575530
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575500
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575515
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575548
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575506
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575512
Pang, Y., Tan, G., Yang, X., Lin, Y., Chen, Y., Zhang, J., Xie, T., Zhou, H., Fang, J., Zhao, Q., et al. (2021) · Figshare · doi:10.6084/m9.figshare.16575545
- Authors
- Farhan, S. M. K., Wang, J., Robinson, J. F., Lahiry, P., Siu, V. M., Prasad, C., Kronick, J. B., Ramsay, D. A., Rupar, C. A., & Hegele, R. A.
- Affiliations
- Western University (CA)
- University of Toronto (CA)
- London Health Sciences Centre (CA)
- Corresponding author
- Hegele, Robert A.
- ORCID
- Venue
- Molecular Genetics & Genomic Medicine
- Publisher
- Wiley
- Published
- 2013-11-18
- Volume
- 2
- Issue
- 1
- Pages
- 73-80
- ISSN
- 2324-9269 (ISSN-L)
- PMC
- PMC3907916
- OpenAlex
- W2142473627
- Cited by
- 76
- References
- 24
- Citations by year
- 2026: 2 · 2025: 4 · 2024: 2 · 2023: 4 · 2022: 8 · 2021: 25 · 2020: 6 · 2019: 2 · 2018: 9 · 2017: 5 · 2016: 3 · 2015: 2 · 2014: 4
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Molecular Genetics & Genomic Medicine (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Scholarship@Western (Western University) (submittedVersion)
- Funders
- Heart and Stroke Foundation of Canada
- Genome Canada (OGI-049)
- Ontario Genomics (OGI-049)
- Government of Canada
- Ontario Genomics Institute (OGI-049)
- Canadian Institutes of Health Research (MOP-13430, MOP-79523, CTP-79853, 79853_1, 79523_1, MOP13430, OGI-049)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- NFS1, iron-sulfur cluster assembly, cysteine desulfurase, lactic acidemia, hypotonia, multiple organ failure, homozygosity mapping, Friedreich's ataxia, iron-sulfur proteins
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