ArticleScience advances2025
The SH protein of mumps virus is a druggable pentameric viroporin.
Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- A Chimeric Virus Approach Reveals the Matrix (M) Gene as a Critical Modulator of Mumps Virus Neurovirulence.Vaccines · 2026Article
- Clustered Mumps Cases at a Tertiary Care Centre in New Delhi, India.Indian journal of pediatrics · 2026Article
- Structural Bases for the Unconventional Activity of a Viroporin Channel.Biochemistry · 2026Article
- Whole-genome analysis of mumps virus genotype F in Shandong, China (2006-2018).Frontiers in microbiology · 2026Article
- A Highly Immunogenic and Cross-Reactive Multi-Epitope Vaccine Candidate Against Duck Hepatitis A Virus: Immunoinformatics Design and Preliminary Experimental Validation.International journal of molecular sciences · 2025Article
- The 6-kilodalton peptide 1 of the familyFrontiers in microbiology · 2025Review
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Viral infections are on the rise and drugs targeting viral proteins are needed. Viroporins constitute a growing group of virus-encoded transmembrane oligomeric proteins that allow passage of small molecules across the membrane. Despite sparsity in viroporin structures, recent work has revealed diversity in both the number of transmembrane helices and oligomeric states. Here, we provide evidence that the small hydrophobic protein (SH) from mumps virus is a pentameric viroporin. From extensive biophysical data, a HADDOCK model of full-length SH shows its intracellular C-terminal region to form an extended structure crucial to stabilization of the pentamer. Heterologous expression of wild-type SH and variants in
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