ArticleJournal of virology2013
A transmembrane domain and GxxxG motifs within L2 are essential for papillomavirus infection.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
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Who cites it
69 citing papers in PubMed, 103 citations in OpenAlex.
- 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
- A transmembrane region in EPEC EspZ promotes oligomerization and contributes to survival of infected intestinal epithelial cells.Microbiology spectrum · 2026Article
- The nuclear import receptor importin-7 targets HPV from the Golgi to the nucleus to promote infection.Science advances · 2025Article
- Article
- HPV16 entry requires dynein for minus-end transport and utilizes kinesin Kif11 for plus-end transport along microtubules during mitosis.Journal of virology · 2025Article
- The Natural History of Cervical Cancer and the Case for MicroRNAs: Is Human Papillomavirus Infection the Whole Story?International journal of molecular sciences · 2024Review
- Chemical mapping of the surface interactome of PIEZO1 identifies CADM1 as a modulator of channel inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- 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
- 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
- The emerging roles of retromer and sorting nexins in the life cycle of viruses.Virologica Sinica · 2022Review
- Article
- HPV16 Entry into Epithelial Cells: Running a Gauntlet.Viruses · 2021Review
- Recent Advances in Our Understanding of the Infectious Entry Pathway of Human Papillomavirus Type 16.Microorganisms · 2021Review
- The long and winding road: human papillomavirus entry and subcellular trafficking.Current opinion in virology · 2021Review
- Retromer stabilizes transient membrane insertion of L2 capsid protein during retrograde entry of human papillomavirus.Science advances · 2021Article
- Human Papillomavirus infection requires the CCT Chaperonin Complex.Journal of virology · 2021Article
- Article
- Advances in Targeting HPV Infection as Potential Alternative Prophylactic Means.International journal of molecular sciences · 2021Review
- High resolution cryo EM analysis of HPV16 identifies minor structural protein L2 and describes capsid flexibility.Scientific reports · 2021Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
During cellular invasion, human papillomavirus type 16 (HPV16) must transfer its viral genome (vDNA) across the endosomal membrane prior to its accumulation at nuclear PML bodies for the establishment of infection. After cellular uptake, the capsid likely undergoes pH-dependent disassembly within the endo-/lysosomal compartment, thereby exposing hidden domains in L2 that facilitate membrane penetration of L2/vDNA complexes. In an effort to identify regions of L2 that might physically interact with membranes, we have subjected the L2 sequence to multiple transmembrane (TM) domain prediction algorithms. Here, we describe a conserved TM domain within L2 (residues 45 to 67) and investigate its role in HPV16 infection. In vitro, the predicted TM domain adopts an alpha-helical structure in lipid environments and can function as a real TM domain, although not as efficiently as the bona fide TM domain of PDGFR. An L2 double point mutant renders the TM domain nonfunctional and blocks HPV16 infection by preventing endosomal translocation of vDNA. The TM domain contains three highly conserved GxxxG motifs. These motifs can facilitate homotypic and heterotypic interactions between TM helices, activities that may be important for vDNA translocation. Disruption of some of these GxxxG motifs resulted in noninfectious viruses, indicating a critical role in infection. Using a ToxR-based homo-oligomerization assay, we show a propensity for this TM domain to self-associate in a GxxxG-dependent manner. These data suggest an important role for the self-associating L2 TM domain and the conserved GxxxG motifs in the transfer of vDNA across the endo-/lysosomal membrane.
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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.