Evidence map›Paper›PMID 41414696›Full record

ArticleACS infectious diseases2026

Polyanionic Sugars Drastically Affect Assembly of Human Papilloma Virus Virus-Like Particles.

Angela Patterson, Kim Young, MacRyan P Biever, Shelby M Klein, Stephen C Jacobson, Martin F Jarrold, Adam Zlotnick

Abstract read
In one paragraph

Article in ACS infectious diseases, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Angela PattersonMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana 47405-7102, United States.
Kim YoungMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana 47405-7102, United States.
MacRyan P BieverDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405-7003, United States.
Shelby M KleinDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405-7003, United States.
Stephen C JacobsonDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405-7003, United States.ORCID 0000-0003-2415-041X
Martin F JarroldDepartment of Chemistry, Indiana University, Bloomington, Indiana 47405-7003, United States.ORCID 0000-0001-7084-176X
Adam ZlotnickMolecular and Cellular Biochemistry Department, Indiana University, Bloomington, Indiana 47405-7102, United States.ORCID 0000-0001-9945-6267

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
NIAID NIH HHS R01 AI118933NIAID NIH HHS R01 AI144022NIGMS NIH HHS R35 GM141922
6 · The paper itself

Abstract

The L1 capsid protein of Human papilloma virus 16 (HPV16) forms pentamers that assemble into virus-like particles (VLPs). With many viruses, interaction of the virus with polysaccharides modulates association of the virus with a host cell. For HPV16, soluble polyanionic saccharides heparin and carrageenan bind to L1 and inhibit cell entry. Based on the observed multivalent binding of heparin, we hypothesized that anionic polysaccharides could act as scaffolds to promote VLP assembly. We observed that heparin, a highly sulfated, flexible polymer, increased the initial rate of assembly and stabilized assembled L1 VLPs. Heparin also notably increased the susceptibility of L1 pentamers to proteolysis. Conversely, κ-carrageenan, a less sulfated, rigid polymer, blocked assembly and destabilized VLPs. We examined the effects of a small panel of anions on assembly to identify their important features. We observed that smaller anions required much higher concentration for an effect, and that their chemical nature also had an impact. These data demonstrate that artificial binding partners can control VLP assembly through their interaction with the exterior of capsid protein and that structural details beyond size and electrostatics are critical to accelerating or inhibiting self-assembly.

Indexed as

Capsid ProteinsHuman papillomavirus 16PolymersVirionVirus AssemblyCarrageenanHeparinHuman Papillomavirus VirusesHumansOncogene Proteins, ViralPolyelectrolytesCapsid ProteinsCarrageenanHeparinL1 protein, Human papillomavirus type 16Oncogene Proteins, ViralPolyelectrolytesPolymerscapsidheparinhuman papilloma virusself-assemblyvirus-like particle

Identifiers

PMID41414696
PMCPMC13108601

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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.