Evidence map›Paper›PMID 22156517›Full record

ArticleJournal of virology2012

A highly conserved residue in the C-terminal helix of HIV-1 matrix is required for envelope incorporation into virus particles.

Laura Brandano, Mario Stevenson

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed, 1 pooled it
1.1field-weighted citation impact, top 26% 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

24 citing papers in PubMed, 1 synthesis or guideline pooled it, 31 citations in OpenAlex.

  1. HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016
    Pooled it
  2. Article
  3. The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation.bioRxiv : the preprint server for biology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Biochemical evidence of a role for matrix trimerization in HIV-1 envelope glycoprotein incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. A structural perspective of compensatory evolution.Current opinion in structural biology · 2014
    Review
  19. Article
  20. Article
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

2 authors at 2 institutions in 1 country.

Laura BrandanoUniversity of Massachusetts Medical School, Worcester, Massachusetts, USA.
Mario Stevenson
University of Massachusetts Chan Medical School · USUniversity of Miami · US

Funding

FUNCTION FOR VPR AND VPX OF PRIMATE LENTIVIRUSESR37AI037475 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEVENSON, MARIO · 2000 to 2009
$3.6M
ROLE OF HIV-1 GAG MA IN VIRAL ENTRYR01AI032890 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEVENSON, MARIO · 1992 to 2011
$3.3M
FUNCTION FOR VPR AND VPX OF PRIMATE LENTIVIRUSESR01AI037475 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEVENSON, MARIO · 1995 to 1999
–
NIAID NIH HHS AI32890NIAID NIH HHS AI37475NIAID NIH HHS R01 AI032890NIAID NIH HHS R01 AI037475NIAID NIH HHS R37 AI037475
6 · The paper itself

Abstract

The incorporation of viral envelope (Env) glycoproteins into nascent particles is an essential step in the production of infectious human immunodeficiency virus type 1 (HIV-1). This process has been shown to require interactions between Env and the matrix (MA) domain of the Gag polyprotein. Previous studies indicate that several residues in the N-terminal region of MA are required for Env incorporation. However, the precise mechanism by which Env proteins are acquired during virus assembly has yet to be fully defined. Here, we examine whether a highly conserved glutamate at position 99 in the C-terminal helix is required for MA function and HIV-1 replication. We analyze a panel of mutant viruses that contain different amino acid substitutions at this position using viral infectivity studies, virus-cell fusion assays, and immunoblotting. We find that E99V mutant viruses are defective for fusion with cell membranes and thus are noninfectious. We show that E99V mutant particles of HIV-1 strains LAI and NL4.3 lack wild-type levels of Env proteins. We identify a compensatory substitution in MA residue 84 and show that it can reverse the E99V-associated defects. Taken together, these results indicate that the C-terminal hydrophobic pocket of MA, which encompasses both residues 84 and 99, has a previously unsuspected and key role in HIV-1 Env incorporation.

Indexed as

Virus ReplicationAmino Acid MotifsAmino Acid SequenceCell LineConserved Sequenceenv Gene Products, Human Immunodeficiency Virusgag Gene Products, Human Immunodeficiency VirusHIV-1HIV InfectionsHumansMolecular Sequence DataProtein BindingProtein Structure, SecondarySequence Alignmentenv Gene Products, Human Immunodeficiency Virusgag Gene Products, Human Immunodeficiency Virus

Identifiers

PMID22156517
PMCPMC3302379
OpenAlexW2073453856

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.