ArticleScience advances2024
Site-specific sulfations regulate the physicochemical properties of papillomavirus-heparan sulfate interactions for entry.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Multivalency influences virus dynamics at the glycocalyx: A study of glycosaminoglycan binding in HPV16 entry.Biophysical journal · 2026Article
- Filamentous virions act as non-infectious interfering particles to modulate papillomavirus infection.Journal of virology · 2026Article
- Polyanionic Sugars Drastically Affect Assembly of Human Papilloma Virus Virus-Like Particles.ACS infectious diseases · 2026Article
- The actin nucleation promoting factor WASH facilitates clathrin-independent endocytosis of human papillomaviruses.EMBO reports · 2025Article
- Glycosaminoglycans as Polyelectrolytes: Charge, Interactions, and Applications.Chembiochem : a European journal of chemical biology · 2025Review
- Article
- Variant-Specific Interactions at the Plasma Membrane: Heparan Sulfate's Impact on SARS-CoV-2 Binding Kinetics.Analytical chemistry · 2025Article
- HSPG-binding peptide Pep19-2.5 is a potent inhibitor of HPV16 infection.Antimicrobial agents and chemotherapy · 2025Article
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Certain human papillomaviruses (HPVs) are etiological agents for several anogenital and oropharyngeal cancers. During initial infection, HPV16, the most prevalent cancer-causing type, specifically interacts with heparan sulfates (HSs), not only enabling initial cell attachment but also triggering a crucial conformational change in viral capsids termed structural activation. It is unknown, whether these HPV16-HS interactions depend on HS sulfation patterns. Thus, we probed potential roles of HS sulfations using cell-based functional and physicochemical assays, including single-molecule force spectroscopy. Our results demonstrate that N-sulfation of HS is crucial for virus binding and structural activation by providing high-affinity sites, and that additional 6O-sulfation is required to mechanically stabilize the interaction, whereas 2O-sulfation and 3O-sulfation are mostly dispensable. Together, our findings identify the contribution of HS sulfation patterns to HPV16 binding and structural activation and reveal how distinct sulfation groups of HS synergize to facilitate HPV16 entry, which, in turn, likely influences the tropism of HPVs.
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