This research received no external funding. Conceptualization, E.M. and S.E.; methodology, E.M., D.T. and P.M.; software, E.M. and A.B.; writing—original draft preparation, E.M., S.E. and D.T.; writing—review and editing, A.B. and P.M. All authors have read and agreed to the published version of the manuscript.
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The intermediate Δ5,3-ketosteroid remains bound to the enzyme with nascent NADH, and the actual presence of NADH in the cofactor-binding site leads to the activation of the Δ5-Δ4-isomerase activity [5,7]. Due to the rarity of the disease, the phenotype–genotype correlation has not been fully investigated in a large case series. Albeit, in general, the functional and biochemical data are in agreement with the expressed phenotype, the clinical phenotype in the affected patients is significantly heterogeneous; moreover, identical DNA variants have been found in the HSD3B2 gene in patients showing a different clinical outcome [3,21,22]. Among others, in a recent work by Ladjouze et al., the authors report the finding of the same mutation (c.665C>A) both in a patient showing a salt-wasting form and in a patient showing a non-salt-wasting form [21]. Taking the above into account and also considering the role of other factors on gene expression (such as epigenetic modifications and other modifying genes), the observation of diverse clinical presentations in these two siblings sharing the same variants is not surprising [23]. We report the presence of two novel variants on the HSD3B2 gene in the compound heterozygous form that likely caused the 3βHSD2 deficiency with variable expressivity in two siblings, a missense mutation on exon 4 (c.370 A>G) and an intronic mutation on intron 3 (c.308-6 G>A), whose potential pathogenetic effect were evaluated by in-silico analysis and need functional validation. App marjosport.
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