ArticleTraffic (Copenhagen, Denmark)2012
Human papillomavirus L2 facilitates viral escape from late endosomes via sorting nexin 17.
Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
105 citing papers in PubMed.
- Inhibition of Langerhans cell maturation by human papillomavirus type 16: a novel role for the annexin A2 heterotetramer in immune suppression.Journal of immunology (Baltimore, Md. : 1950) · 2014Trial
- Regulation of HPV-16 infection by ubiquitination of the L1 major capsid protein.Journal of virology · 2026Article
- Cargo-Adaptor Cooperation Programs Retromer Coat Architecture.bioRxiv : the preprint server for biology · 2026Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- The nuclear import receptor importin-7 targets HPV from the Golgi to the nucleus to promote infection.Science advances · 2025Article
- Article
- SNX11 Deletion Inhibits Dabie bandavirus Infection by Interfering with the Assembly of V-ATPase.Pathogens (Basel, Switzerland) · 2025Article
- AlphaFold models of host-pathogen interactions elucidate the prevalence and structural modes of molecular mimicry.bioRxiv : the preprint server for biology · 2025Article
- Article
- Sexually transmitted human papillomavirus and related sequelae.Clinical microbiology reviews · 2025Review
- HPV and Cervical Cancer-Biology, Prevention, and Treatment Updates.Current oncology (Toronto, Ont.) · 2025Review
- HPV16 entry requires dynein for minus-end transport and utilizes kinesin Kif11 for plus-end transport along microtubules during mitosis.Journal of virology · 2025Article
- Article
- The Intricate Interplay between APOBEC3 Proteins and DNA Tumour Viruses.Pathogens (Basel, Switzerland) · 2024Review
- Emerging Role of Sorting Nexin 17 in Human Health and Disease.Current protein & peptide science · 2024Review
- SNX27:Retromer:ESCPE-1-mediated early endosomal tubulation impacts cytomegalovirus replication.Frontiers in cellular and infection microbiology · 2024Article
- Metabolic Profiling, Antiviral Activity and the Microbiome of Some Mauritian Soft Corals.Marine drugs · 2023Article
- Sequence-independent activity of a predicted long disordered segment of the human papillomavirus type 16 L2 capsid protein during virus entry.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Noncanonical Rab9a action supports retromer-mediated endosomal exit of human papillomavirus during virus entry.PLoS pathogens · 2023Article
- Exploring the link between viruses and cancer in companion animals: a comprehensive and comparative analysis.Infectious agents and cancer · 2023Review
45 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
The human papillomavirus (HPV) L2 capsid protein plays an essential role during the early stages of viral infection, but the molecular mechanisms underlying its mode of action remain obscure. Using a proteomic approach, we have identified the adaptor protein, sorting nexin 17 (SNX17) as a strong interacting partner of HPV L2. This interaction occurs through a highly conserved SNX17 consensus binding motif, which is present in the majority of HPV L2 proteins analysed. Using mutants of L2 defective for SNX17 interaction, or siRNA ablation of SNX17 expression, we demonstrate that the interaction between L2 and SNX17 is essential for viral infection. Furthermore, loss of the L2-SNX17 interaction results in enhanced turnover of the L2 protein and decreased stability of the viral capsids, and concomitantly, there is a dramatic decrease in the efficiency with which viral genomes transit to the nucleus. Indeed, using a range of endosomal and lysosomal markers, we show that capsids defective in their capacity to bind SNX17 transit much more rapidly to the lysosomal compartment. These results demonstrate that the L2-SNX17 interaction is essential for viral infection and facilitates the escape of the L2-DNA complex from the late endosomal/lysosomal compartments.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.