Evidence map›Paper›PMID 11602751›Full record

ArticleJournal of virology2001

Identification of aleutian mink disease parvovirus capsid sequences mediating antibody-dependent enhancement of infection, virus neutralization, and immune complex formation.

M E Bloom, S M Best, S F Hayes, R D Wells, J B Wolfinbarger, R McKenna, M Agbandje-McKenna

Abstract read
In one paragraph

Article in Journal of virology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
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  5. Structures and functions of the limited natural polyclonal antibody response to parvovirus infection.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  15. Structure-guided evolution of antigenically distinct adeno-associated virus variants for immune evasion.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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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

7 authors at 3 institutions in 1 country.

M E BloomLaboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, Montana 59840, USA. mbloom@niaid.nih.gov
S M Best
S F Hayes
R D Wells
J B Wolfinbarger
R McKenna
M Agbandje-McKenna
Global Viral · USNational Institute of Allergy and Infectious Diseases · USUniversity of Florida · US

Funding

PATHOGENESIS OF ALEUTIAN MINK DISEASE PARVOVIRUS INFECTIONSZ01AI000085 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI BLOOM, MARSHALL · 1985 to 2004
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6 · The paper itself

Abstract

Aleutian mink disease parvovirus (ADV) causes a persistent infection associated with circulating immune complexes, immune complex disease, hypergammaglobulinemia, and high levels of antiviral antibody. Although antibody can neutralize ADV infectivity in Crandell feline kidney cells in vitro, virus is not cleared in vivo, and capsid-based vaccines have proven uniformly ineffective. Antiviral antibody also enables ADV to infect macrophages, the target cells for persistent infection, by Fc-receptor-mediated antibody-dependent enhancement (ADE). The antibodies involved in these unique aspects of ADV pathogenesis may have specific targets on the ADV capsid. Prominent differences exist between the structure of ADV and other, more-typical parvoviruses, which can be accounted for by short peptide sequences in the flexible loop regions of the capsid proteins. In order to determine whether these short sequences are targets for antibodies involved in ADV pathogenesis, we studied heterologous antibodies against several peptides present in the major capsid protein, VP2. Of these antibodies, a polyclonal rabbit antibody to peptide VP2:428-446 was the most interesting. The anti-VP2:428-446 antibody aggregated virus particles into immune complexes, mediated ADE, and neutralized virus infectivity in vitro. Thus, antibody against this short peptide can be implicated in key facets of ADV pathogenesis. Structural modeling suggested that surface-exposed residues of VP2:428-446 are readily accessible for antibody binding. The observation that antibodies against a single target peptide in the ADV capsid can mediate both neutralization and ADE may explain the failure of capsid-based vaccines.

Indexed as

Aleutian Mink DiseaseAleutian Mink Disease VirusAmino Acid SequenceAnimalsAntibodies, ViralAntigen-Antibody ComplexCapsidCatsCell LineFluorescent Antibody Technique, IndirectHumansImmunoblottingMicroscopy, ImmunoelectronMolecular Sequence DataNeutralization TestsPeptide FragmentsAntibodies, ViralAntigen-Antibody ComplexPeptide Fragments

Identifiers

PMID11602751
PMCPMC114691
OpenAlexW2064788762

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.