ArticleJournal of virology2018
Extracellular Conformational Changes in the Capsid of Human Papillomaviruses Contribute to Asynchronous Uptake into Host Cells.
Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
33 citing papers in PubMed, 50 citations in OpenAlex.
- Multivalency influences virus dynamics at the glycocalyx: A study of glycosaminoglycan binding in HPV16 entry.Biophysical journal · 2026Article
- Article
- Filamentous virions act as non-infectious interfering particles to modulate papillomavirus infection.Journal of virology · 2026Article
- The actin nucleation promoting factor WASH facilitates clathrin-independent endocytosis of human papillomaviruses.EMBO reports · 2025Article
- The nuclear import receptor importin-7 targets HPV from the Golgi to the nucleus to promote infection.Science advances · 2025Article
- Article
- Human Papillomavirus Type 16 Stimulates WAVE1- and WAVE2-Dependent Actin Protrusions for Endocytic Entry.Viruses · 2025Article
- HSPG-binding peptide Pep19-2.5 is a potent inhibitor of HPV16 infection.Antimicrobial agents and chemotherapy · 2025Article
- Glycan-induced structural activation softens the human papillomavirus capsid for entry through reduction of intercapsomere flexibility.Nature communications · 2024Article
- Site-specific sulfations regulate the physicochemical properties of papillomavirus-heparan sulfate interactions for entry.Science advances · 2024Article
- The BICD2 dynein cargo adaptor binds to the HPV16 L2 capsid protein and promotes HPV infection.PLoS pathogens · 2024Article
- Article
- Master mitotic kinases regulate viral genome delivery during papillomavirus cell entry.Nature communications · 2023Article
- HPV is a cargo for the COPI sorting complex during virus entry.Science advances · 2023Article
- Heparan Sulfate and Sialic Acid in Viral Attachment: Two Sides of the Same Coin?International journal of molecular sciences · 2022Review
- Proteases and HPV-Induced Carcinogenesis.Cancers · 2022Review
- HPV16 Entry into Epithelial Cells: Running a Gauntlet.Viruses · 2021Review
- Kallikreins emerge as new regulators of viral infections.Cellular and molecular life sciences : CMLS · 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human papillomavirus 16 (HPV16) is the leading cause of cervical cancer. For initial infection, HPV16 utilizes a novel endocytic pathway for host cell entry. Unique among viruses, uptake occurs asynchronously over a protracted period of time, with half-times between 9 and 12 h. To trigger endocytic uptake, the virus particles need to undergo a series of structural modifications after initial binding to heparan sulfate proteoglycans (HSPGs). These changes involve proteolytic cleavage of the major capsid protein L1 by kallikrein-8 (KLK8), exposure of the N terminus of the minor capsid protein L2 by cyclophilins, and cleavage of this N terminus by furin. Overall, the structural changes are thought to facilitate the engagement of an elusive secondary receptor for internalization. Here, we addressed whether structural changes are the rate-limiting steps during infectious internalization of HPV16 by using structurally primed HPV16 particles. Our findings indicate that the structural modifications mediated by cyclophilins and furin, which lead to exposure and cleavage, respectively, of the L2 N terminus contribute to the slow and asynchronous internalization kinetics, whereas conformational changes elicited by HSPG binding and KLK8 cleavage did not. However, these structural modifications accounted for only 30 to 50% of the delay in internalization. Therefore, we propose that limited internalization receptor availability for engagement of HPV16 causes slow and asynchronous internalization in addition to rate-limiting structural changes in the viral capsid.
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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.