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Mutation near the binding interfaces at α-hemoglobin stabilizing protein is highly pathogenic.

Jesu Francis Borgio1, Mohammed S Al-Madan2, Sayed AbdulAzeez1

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Summary

Alpha hemoglobin stabilizing protein (AHSP) mutations can cause harmful reactive oxygen radicals. The V56G substitution in AHSP is identified as highly pathogenic, impacting protein interactions and potentially leading to erythroid cell dysfunction.

Keywords:
bioinformaticsglobin genesinteraction sitesinterface residuesmolecular modelingmutationnsSNPsprotein-protein interactionα-Hemoglobin stabilizing protein (AHSP)

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Free alpha-hemoglobin aggregation generates reactive oxygen species during erythroid cell development.
  • Alpha hemoglobin stabilizing protein (AHSP) acts as a chaperone to prevent this harmful aggregation.
  • Mutations in the AHSP gene can disrupt its interaction with globin proteins, potentially impacting erythroid cell function.

Purpose of the Study:

  • To identify deleterious single nucleotide polymorphisms (nsSNPs) in the AHSP gene.
  • To evaluate the pathogenic effects of these nsSNPs on AHSP-globin interactions.
  • To investigate the impact of specific AHSP mutations on protein stability and interactions with other proteins like HBA2 and KLF1.

Main Methods:

  • Utilized multiple computational tools (PROVEAN, SIFT, SNAP2, SNPs&GO, PolyPhen, FATHMM, PANTHER, VEST) to predict the pathogenicity of nsSNPs in AHSP.
  • Performed protein-protein interaction analysis to assess the effect of mutations on AHSP's binding capabilities.
  • Analyzed changes in binding energies associated with AHSP and HBA1 gene mutations.

Main Results:

  • The V56G substitution in AHSP was consistently identified as the most pathogenic nsSNP across all computational tools.
  • This V56G mutation occurs near a hotspot, forms an extra helix, and significantly disrupts the interaction between AHSP and proteins like HBA2 and KLF1.
  • Significant variations in binding energies were observed for mutations in the AHSP and/or HBA1 genes.

Conclusions:

  • The V56G mutation in AHSP (p.val56Gly) is a highly pathogenic variant with significant implications for AHSP-globin interactions.
  • This mutation disrupts normal protein interactions, potentially contributing to erythroid cell dysfunction.
  • The study recommends further experimental validation of the p.val56Gly mutation in wet lab settings.