Evidence map›Paper›PMID 23536685›Full record

ReviewJournal of virology2013

The evolving field of human papillomavirus receptor research: a review of binding and entry.

Adam B Raff, Andrew W Woodham, Laura M Raff, Joseph G Skeate, Lisa Yan, Diane M Da Silva, Mario Schelhaas, W Martin Kast

Open access · bronzeAbstract readReview
In one paragraph

Review 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 108 papers.

0numbers the graph read from it
0cells of the map it votes in
108citing papers in PubMed
9.9field-weighted citation impact, top 1% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

108 citing papers in PubMed, 180 citations in OpenAlex.

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48 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Adam B RaffNorris Comprehensive Cancer Center, University of Southern California, Los Angeles, Los Angeles, California, USA.
Andrew W Woodham
Laura M Raff
Joseph G Skeate
Lisa Yan
Diane M Da Silva
Mario Schelhaas
W Martin Kast
University of Southern California · USUniversity of Münster · DE

Funding

USC/NORRIS COMPREHENSIVE CANCER CENTER (CORE) SUPPORTP30CA014089 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Fumito Ito · 1985 to 2026
$181.4M
Southern California Clinical and Translational Science InstituteUL1TR000130 · NCATS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI BUCHANAN, THOMAS A · 2012 to 2015
$36.0M
VLP VACCINES AGAINST HPV INDUCED TUMORSR01CA074397 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI KAST, WIJBE MARTIN · 1997 to 2020
$5.5M
Southern California Clinical and Translational Science InstituteTL1TR000132 · NCATS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI BUCHANAN, THOMAS A · 2012 to 2014
$491k
NCATS NIH HHS TL1 TR000132NCATS NIH HHS TL1TR000132NCATS NIH HHS UL1 TR000130NCI NIH HHS P30 CA014089NCI NIH HHS P30CA014089NCI NIH HHS R01 CA074397
6 · The paper itself

Abstract

Human papillomaviruses (HPVs) infect epithelia and can lead to the development of lesions, some of which have malignant potential. HPV type 16 (HPV16) is the most oncogenic genotype and causes various types of cancer, including cervical, anal, and head and neck cancers. However, despite significant research, our understanding of the mechanism by which HPV16 binds to and enters host cells remains fragmented. Over several decades, many HPV receptors and entry pathways have been described. This review puts those studies into context and offers a model of HPV16 binding and entry as a framework for future research. Our model suggests that HPV16 binds to heparin sulfate proteoglycans (HSPGs) on either the epithelial cell surface or basement membrane through interactions with the L1 major capsid protein. Growth factor receptors may also become activated through HSPG/growth factor/HPV16 complexes that initiate signaling cascades during early virion-host cell interactions. After binding to HSPGs, the virion undergoes conformational changes, leading to isomerization by cyclophilin B and proprotein convertase-mediated L2 minor capsid protein cleavage that increases L2 N terminus exposure. Along with binding to HSPGs, HPV16 binds to α6 integrins, which initiate further intracellular signaling events. Following these primary binding events, HPV16 binds to a newly identified L2-specific receptor, the annexin A2 heterotetramer. Subsequently, clathrin-, caveolin-, lipid raft-, flotillin-, cholesterol-, and dynamin-independent endocytosis of HPV16 occurs.

Indexed as

Virus InternalizationAlphapapillomavirusAnimalsHeparan Sulfate ProteoglycansHuman papillomavirus 16HumansPapillomavirus InfectionsReceptors, VirusHeparan Sulfate ProteoglycansReceptors, Virus

Identifiers

PMID23536685
PMCPMC3648114
OpenAlexW2105035717

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.