Evidence map›Paper›PMID 18657545›Full record

ArticleJournal of molecular biology2008

Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting.

Jamil S Saad, Sherimay D Ablan, Ruba H Ghanam, Andrew Kim, Kalola Andrews, Kunio Nagashima, Ferri Soheilian, Eric O Freed, Michael F Summers

Abstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
2.8field-weighted citation impact, top 8% 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

79 citing papers in PubMed, 98 citations in OpenAlex.

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  11. Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2022
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19 more citing papers are in PubMed but not listed here.

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 at 5 institutions in 1 country.

Jamil S SaadHoward Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland Baltimore County, 1000 Hilltop Circle, Baltimore, MD 21250, USA.
Sherimay D Ablan
Ruba H Ghanam
Andrew Kim
Kalola Andrews
Kunio Nagashima
Ferri Soheilian
Eric O Freed
Michael F Summers
Howard Hughes Medical Institute · USFrederick National Laboratory for Cancer Research · USNational Cancer Institute · USScience Applications International Corporation (United States) · USUniversity of Maryland, Baltimore County · US

Funding

NMR STUDIES OF HIV1 PROTEINSR37AI030917 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE COUNTY · PI SUMMERS, MICHAEL FINLEY · 1997 to 2015
$4.9M
Retroviral Gag Trafficking, Env Incorporation, and Virus AssemblyZ01BC010775 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FREED, ERIC · 2007 to 2008
$961k
Retrovirus Budding and Endosomal SortingZ01BC010776 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI FREED, ERIC · 2007 to 2008
$899k
NMR STUDIES OF HIV-1 PROTEINSR01AI030917 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI SUMMERS, MICHAEL F. · 1991 to 1996
–
Howard Hughes Medical InstituteIntramural NIH HHS Z01 BC010775Intramural NIH HHS Z01 BC010776NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400NIAID NIH HHS AI30917NIAID NIH HHS R37 AI030917
6 · The paper itself

Abstract

During the late phase of retroviral replication, newly synthesized Gag proteins are targeted to the plasma membrane (PM), where they assemble and bud to form immature virus particles. Membrane targeting by human immunodeficiency virus type 1 (HIV-1) Gag is mediated by the PM marker molecule phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P(2)], which is capable of binding to the matrix (MA) domain of Gag in an extended lipid conformation and of triggering myristate exposure. Here, we show that, as observed previously for HIV-1 MA, the myristyl group of HIV-2 MA is partially sequestered within a narrow hydrophobic tunnel formed by side chains of helices 1, 2, 3, and 5. However, the myristate of HIV-2 MA is more tightly sequestered than that of the HIV-1 protein and does not exhibit concentration-dependent exposure. Soluble PI(4,5)P(2) analogs containing truncated acyl chains bind HIV-2 MA and induce minor long-range structural changes but do not trigger myristate exposure. Despite these differences, the site of HIV-2 assembly in vivo can be manipulated by enzymes that regulate PI(4,5)P(2) localization. Our findings indicate that HIV-1 and HIV-2 are both targeted to the PM for assembly via a PI(4,5)P(2)-dependent mechanism, despite differences in the sensitivity of the MA myristyl switch, and suggest a potential mechanism that may contribute to the poor replication kinetics of HIV-2.

Indexed as

Protein ConformationAnimalsCell MembraneHIV-2HumansModels, MolecularMyristatesNuclear Magnetic Resonance, BiomolecularPhosphatidylinositol 4,5-DiphosphateViral ProteinsVirus ReplicationMyristatesPhosphatidylinositol 4,5-DiphosphateViral Proteins

Identifiers

PMID18657545
PMCPMC2581411
OpenAlexW2154140185

What OpenQuestion holds

Textmetadata
LicenceTDM
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.