Evidence map›Paper›PMID 14610182›Full record

ArticleJournal of virology2003

Human immunodeficiency virus type 1 N-terminal capsid mutants containing cores with abnormally high levels of capsid protein and virtually no reverse transcriptase.

Shixing Tang, Tsutomu Murakami, Naiqian Cheng, Alasdair C Steven, Eric O Freed, Judith G Levin

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
1.3field-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

38 citing papers in PubMed, 52 citations in OpenAlex.

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  10. The cyclosporin A washout assay to detect HIV-1 uncoating in infected cells.Methods in molecular biology (Clifton, N.J.) · 2014
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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

6 authors at 3 institutions in 3 countries.

Shixing TangLaboratory of Molecular Genetics, National Institute of Child Health and Human Development, Bethesda, Maryland 20892, USA.
Tsutomu Murakami
Naiqian Cheng
Alasdair C Steven
Eric O Freed
Judith G Levin
Laboratory of Molecular Genetics · PLNational Institute of Allergy and Infectious Diseases · USNational Institute of Arthritis and Musculoskeletal and Skin Diseases · US

Funding

Structural Biology Of Virus AssemblyZIAAR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI WINGFIELD, PAUL T · 2009 to 2024
$19.2M
Molecular Genetics Of Mammalian Retrovirus ReplicationZIAHD000069 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI LEVIN, JUDITH G · 2009 to 2015
$7.2M
STRUCTURAL BIOLOGY OF VIRUS ASSEMBLYZ01AR027002 · NIAMS · NATIONAL INSTITUTE OF ARTHRITIS AND MUSCULOSKELETAL AND SKIN DISEASES · PI STEVEN, ALASDAIR C. · 1987 to 2008
$3.0M
MOLECULAR GENETICS OF MAMMALIAN RETROVIRUS REPLICATIONZ01HD000069 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI LEVIN, JUDITH G · 1985 to 2008
$1.8M
Hiv 1 Gag And Env Proteins In Virus Assembly/ InfectionZ01AI000772 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI FREED, ERIC O · 1997 to 2003
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6 · The paper itself

Abstract

We previously described the phenotype associated with three alanine substitution mutations in conserved residues (Trp23, Phe40, and Asp51) in the N-terminal domain of human immunodeficiency virus type 1 capsid protein (CA). All of the mutants produce noninfectious virions that lack conical cores and, despite having a functional reverse transcriptase (RT), are unable to initiate reverse transcription in vivo. Here, we have focused on elucidating the mechanism by which these CA mutations disrupt virus infectivity. We also report that cyclophilin A packaging is severely reduced in W23A and F40A virions, even though these residues are distant from the cyclophilin A binding loop. To correlate loss of infectivity with a possible defect in an early event preceding reverse transcription, we modeled disassembly by generating viral cores from particles treated with mild nonionic detergent; cores were isolated by sedimentation in sucrose density gradients. In general, fractions containing mutant cores exhibited a normal protein profile. However, there were two striking differences from the wild-type pattern: mutant core fractions displayed a marked deficiency in RT protein and enzymatic activity (<5% of total RT in gradient fractions) and a substantial increase in the retention of CA. The high level of core-associated CA suggests that mutant cores may be unable to undergo proper disassembly. Thus, taken together with the almost complete absence of RT in mutant cores, these findings can account for the failure of the three CA mutants to synthesize viral DNA following virus entry into cells.

Indexed as

MutationCapsid ProteinsDNA, ViralHIV-1HIV Reverse TranscriptaseMembrane FusionMicroscopy, ElectronModels, MolecularViral Core ProteinsVirulenceCapsid ProteinsDNA, ViralHIV Reverse TranscriptaseViral Core Proteins

Identifiers

PMID14610182
PMCPMC262599
OpenAlexW2165481479

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.