ArticleViruses2022
Human Papillomavirus L2 Capsid Protein Stabilizes γ-Secretase during Viral Infection.
Article in Viruses, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- The nuclear import receptor importin-7 targets HPV from the Golgi to the nucleus to promote infection.Science advances · 2025Article
- Article
- Cell-Free Expression of HPV16 Minor Capsid Protein L2 and Its Interaction with S100A10.Protein and peptide letters · 2025Article
- Article
- The BICD2 dynein cargo adaptor binds to the HPV16 L2 capsid protein and promotes HPV infection.PLoS pathogens · 2024Article
- Elevated A-to-I RNA editing in COVID-19 infected individuals.NAR genomics and bioinformatics · 2023Article
- Human papillomavirus associated cervical lesion: pathogenesis and therapeutic interventions.MedComm · 2023Review
- Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry.PLoS pathogens · 2023Article
- Crystal Structures of Plk1 Polo-Box Domain Bound to the Human Papillomavirus Minor Capsid Protein L2-Derived Peptide.Journal of microbiology (Seoul, Korea) · 2023Article
- HPV is a cargo for the COPI sorting complex during virus entry.Science advances · 2023Article
- Human Papillomavirus Minor Capsid Protein L2 Mediates Intracellular Trafficking into and Passage beyond the Endoplasmic Reticulum.Microbiology spectrum · 2022Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Intracellular trafficking of human papillomavirus (HPV) during virus entry requires γ-secretase, a cellular protease consisting of a complex of four cellular transmembrane (TM) proteins. γ-secretase typically cleaves substrate proteins but it plays a non-canonical role during HPV entry. γ-secretase binds to the HPV minor capsid protein L2 and facilitates its insertion into the endosomal membrane. After insertion, L2 protrudes into the cytoplasm, which allows HPV to bind other cellular factors required for proper virus trafficking into the retrograde transport pathway. Here, we further characterize the interaction between γ-secretase and HPV L2. We show that γ-secretase is required for cytoplasmic protrusion of L2 and that L2 associates strongly with the PS1 catalytic subunit of γ-secretase and stabilizes the γ-secretase complex. Mutational studies revealed that a putative TM domain in HPV16 L2 cannot be replaced by a foreign TM domain, that infectivity of HPV TM mutants is tightly correlated with γ-secretase binding and stabilization, and that the L2 TM domain is required for protrusion of the L2 protein into the cytoplasm. These results provide new insight into the interaction between γ-secretase and L2 and highlight the importance of the native HPV L2 TM domain for proper virus trafficking during entry.
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