Liza Eiman
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Research Subjects
Liza Eiman has a total of 7 co-authors. Here are the top co-authors by number of shared publications:
- Farheen Nasir Awan
Department of Biotechnology, Kinnaird College for Women, Lahore 54000, Pakistan
1 shared publication - Hirotsugu Oda
Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, 50923 Cologne, Germany
1 shared publication - Maria Asif
Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), University of Cologne, 50923 Cologne, Germany
1 shared publication - Muhammad Sajid Hussain
Cologne Center for Genomics (CCG), University of Cologne, Faculty of Medicine and University Hospital Cologne, Cologne, Germany
1 shared publication - Niklas Dahl
Department of Immunology, Genetics and Pathology, Uppsala University, Uppsala, Sweden
1 shared publication - Shahid Mahmood Baig
Health Services Academy (HSA), Islamabad 44000, Pakistan
1 shared publication
Latest Publications
- Open Access
Clinical and Molecular Characterization of Pakistani Mucopolysaccharidosis Families with SGSH and GALNS Deficiencies
Background: Mucopolysaccharidoses (MPS) are rare lysosomal storage disorders caused by deficiencies in glycosaminoglycan (GAG)-degrading enzymes, leading to progressive multisystem involvement. Methods: We evaluated two unrelated consanguineous Pakistani families, each with three individuals showing features consistent with MPS. Affected individuals in Family 1 presented with developmental regression, severe cognitive impairment, behavioral abnormalities and facial dysmorphisms. The affected individuals in Family 2 showed classical skeletal dysplasia consistent with Morquio syndrome. Whole-exome sequencing (WES), segregation analysis, and in silico protein modeling were performed to identify and characterize pathogenic gene variants. Results: Analysis of WES data revealed a homozygous missense variant in the SGSH gene [c.548G>A (p.Cys183Tyr)] in the three cases of Family 1 and a homozygous splice-site variant in the GALNS gene (c.423-1G>A) in the cases of Family 2. The SGSH variant, located within the sulfatase catalytic domain and classified as likely pathogenic (ACMG), is consistent with the Sanfilippo A phenotype and represents the first clinical characterization of this allele. Regarding Family 2, we identified the GALNS mutation as a recurrent pathogenic founder allele previously reported in individuals of South Asian descent. Structural modeling of SGSH p.Cys183Tyr predicted disruption of a conserved cysteine residue and altered protein stability, likely supporting its deleterious effect. Conclusions: This study expands the spectrum of MPS-associated variants in Pakistan. The findings underscore the importance of genomic diagnostics for enabling early detection, accurate classification, and genetic counseling in populations with high consanguinity.
Open AccessClinical and Molecular Characterization of Pakistani Mucopolysaccharidosis Families with SGSH and GALNS Deficiencies
Background: Mucopolysaccharidoses (MPS) are rare lysosomal storage disorders caused by deficiencies in glycosaminoglycan (GAG)-degrading enzymes, leading to progressive multisystem involvement. Methods: We evaluated two unrelated consanguineous Pakistani families, each with three individuals showing features consistent with MPS. Affected individuals in Family 1 presented with developmental regression, severe cognitive impairment, behavioral abnormalities and facial dysmorphisms. The affected individuals in Family 2 showed classical skeletal dysplasia consistent with Morquio syndrome. Whole-exome sequencing (WES), segregation analysis, and in silico protein modeling were performed to identify and characterize pathogenic gene variants. Results: Analysis of WES data revealed a homozygous missense variant in the SGSH gene [c.548G>A (p.Cys183Tyr)] in the three cases of Family 1 and a homozygous splice-site variant in the GALNS gene (c.423-1G>A) in the cases of Family 2. The SGSH variant, located within the sulfatase catalytic domain and classified as likely pathogenic (ACMG), is consistent with the Sanfilippo A phenotype and represents the first clinical characterization of this allele. Regarding Family 2, we identified the GALNS mutation as a recurrent pathogenic founder allele previously reported in individuals of South Asian descent. Structural modeling of SGSH p.Cys183Tyr predicted disruption of a conserved cysteine residue and altered protein stability, likely supporting its deleterious effect. Conclusions: This study expands the spectrum of MPS-associated variants in Pakistan. The findings underscore the importance of genomic diagnostics for enabling early detection, accurate classification, and genetic counseling in populations with high consanguinity.