Evidence map›Paper›PMID 39276669›Full record

ArticleVirology2024

Heterogeneity of HPV16 virus-like particles indicates a complex assembly energy surface.

Angela Patterson, Kim Young, MacRyan P Biever, Shelby M Klein, Sheng-Yuan Huang, Pete A DePhillips, Stephen C Jacobson, Martin F Jarrold, Adam Zlotnick

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
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

9 authors.

Angela PattersonMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, IN, USA.
Kim YoungMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, IN, USA.
MacRyan P BieverDepartment of Chemistry, Indiana University, Bloomington, IN, USA.
Shelby M KleinDepartment of Chemistry, Indiana University, Bloomington, IN, USA.
Sheng-Yuan HuangDepartment of Chemistry, Indiana University, Bloomington, IN, USA.
Pete A DePhillipsAnalytical Research and Development, Merck & Co., Inc., Rahway, NJ, 07065, USA.
Stephen C JacobsonDepartment of Chemistry, Indiana University, Bloomington, IN, USA.
Martin F JarroldDepartment of Chemistry, Indiana University, Bloomington, IN, USA.
Adam ZlotnickMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, IN, USA. Electronic address: azlotnic@iu.edu.

Funding

Multimode Observation of Virus Capsid AssemblyR01AI118933 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI Adam Zlotnick · 2016 to 2026
$4.0M
Single-Particle Analysis of Virus Capsids, Bacteria, and Extracellular VesiclesR35GM141922 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI Stephen C Jacobson · 2021 to 2026
$3.5M
The Structural Biology of HBVR01AI144022 · NIAID · TRUSTEES OF INDIANA UNIVERSITY · PI ZLOTNICK, ADAM · 2019 to 2022
$1.5M
HEAT SHOCK PROTEIN GP96 AND IMMUNITYR01AI044022 · NIAID · UNIVERSITY OF ROCHESTER · PI COHEN, NICHOLAS · 2000 to 2003
$1.3M
NIAID NIH HHS R01 AI044022NIAID NIH HHS R01 AI118933NIAID NIH HHS R01 AI144022NIGMS NIH HHS R35 GM141922
6 · The paper itself

Abstract

Human Papillomavirus serotype 16 (HPV16) capsid protein (L1) pentamers canonically assemble into T = 7 icosahedral capsids. Such virus-like particles are the basis of the HPV vaccine. We examined assembly of L1 pentamers in response to pH, mild oxidants, and ionic strength and found a mixture of closed, roughly spherical structures from ∼20 to ∼70 nm in diameter, indicating the presence of many kinetically accessible energy minima. Using bulk and single particle techniques we observed that the size distribution changes but does not reach homogeneity. Though heterogenous in size, particles showed uniform responses to low ionic strength dissociation, thermal unfolding, and susceptibility to protease digestion. These assays suggest maturation over time, but at different rates. Cysteine oxidation further stabilized particles at early, but not late, times without changing general characteristics including thermal stability and protease digestion. These data show complex assembly paths to species of different sizes, but with locally similar interactions.

Indexed as

Capsid ProteinsHuman papillomavirus 16Oncogene Proteins, ViralVirus AssemblyCapsidHumansHydrogen-Ion ConcentrationOsmolar ConcentrationOxidation-ReductionVirionCapsid ProteinsL1 protein, Human papillomavirus type 16Oncogene Proteins, ViralCapsidCharge detection-mass spectrometryHPV16Human papilloma virusResistive pulse sensingSelf-assembly

Identifiers

PMID39276669
PMCPMC11560593

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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.