Evidence map›Paper›PMID 32315582›Full record

ReviewViral immunology

Parvovirus Capsid-Antibody Complex Structures Reveal Conservation of Antigenic Epitopes Across the Family.

Shanan N Emmanuel, Mario Mietzsch, Yu Shan Tseng, James Kennon Smith, Mavis Agbandje-McKenna

Open access · greenAbstract readReview
In one paragraph

Review in Viral immunology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

31 citing papers in PubMed, 34 citations in OpenAlex.

  1. Distinct evolutionary patterns of endemic and emerging parvoviruses and the origin of a new pandemic virus.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. The amazing AAV capsids: Into the structure-verse.Molecular therapy. Methods & clinical development · 2025
    Review
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  8. Nonclinical strategies and considerations to enable the redosing of gene therapies.Molecular therapy. Methods & clinical development · 2025
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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

5 authors at 1 institution in 1 country.

Shanan N EmmanuelDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, Florida, USA.
Mario MietzschDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, Florida, USA.
Yu Shan TsengDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, Florida, USA.
James Kennon SmithDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, Florida, USA.
Mavis Agbandje-McKennaDepartment of Biochemistry and Molecular Biology, College of Medicine, University of Florida, Gainesville, Florida, USA.
University of Florida · US

Funding

Structural studies of AAV capsids and their glycan receptor interactionsR01GM082946 · NIGMS · UNIVERSITY OF FLORIDA · PI ROBERT MCKENNA · 2007 to 2026
$6.1M
BASIC MICROBIOLOGY &INFECTIOUS DISEASEST32AI007110 · NIAID · UNIVERSITY OF FLORIDA · PI Stephanie M Karst · 1985 to 2026
$4.3M
NIAID NIH HHS T32 AI007110NIGMS NIH HHS R01 GM082946
6 · The paper itself

Abstract

The parvoviruses are small nonenveloped single stranded DNA viruses that constitute members that range from apathogenic to pathogenic in humans and animals. The infection with a parvovirus results in the generation of antibodies against the viral capsid by the host immune system to eliminate the virus and to prevent re-infection. For members currently either being developed as delivery vectors for gene therapy applications or as oncolytic biologics for tumor therapy, efforts are aimed at combating the detrimental effects of pre-existing or post-treatment antibodies that can eliminate therapeutic benefits. Therefore, understanding antigenic epitopes of parvoviruses can provide crucial information for the development of vaccination applications and engineering novel capsids able to escape antibody recognition. This review aims to capture the information for the binding regions of ∼30 capsid-antibody complex structures of different parvovirus capsids determined to date by cryo-electron microscopy and three-dimensional image reconstruction. The comparison of all complex structures revealed the conservation of antigenic regions among parvoviruses from different genera despite low sequence identity and indicates that the available data can be used across the family for vaccine development and capsid engineering.

Indexed as

Capsid ProteinsEpitopesAnimalsAntibodies, ViralCapsidCryoelectron MicroscopyHumansParvovirusVaccine DevelopmentAntibodies, ViralCapsid ProteinsEpitopesbinding epitopescryo-EM and 3D image reconstructionneutralizing antibodiesparvovirusesviral vectors

Identifiers

PMID32315582
PMCPMC8020512
OpenAlexW3017097499

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.