Evidence map›Paper›PMID 18792916›Full record

ArticleJournal of cellular physiology2009

Role of the feline immunodeficiency virus L-domain in the presence or absence of Gag processing: involvement of ubiquitin and Nedd4-2s ligase in viral egress.

Arianna Calistri, Claudia Del Vecchio, Cristiano Salata, Michele Celestino, Marta Celegato, Heinrich Göttlinger, Giorgio Palù, Cristina Parolin

Open access · greenAbstract readComparative Study
In one paragraph

Article in Journal of cellular physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

26 citing papers in PubMed, 33 citations in OpenAlex.

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  15. Article
  16. Virus budding and the ESCRT pathway.Cell host & microbe · 2013
    Review
  17. Article
  18. Review
  19. Article
  20. How ubiquitin functions with ESCRTs.Traffic (Copenhagen, Denmark) · 2011
    Review
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

8 authors at 2 institutions in 2 countries.

Arianna CalistriDepartment of Histology, Microbiology and Medical Biotechnologies, Section of Microbiology and Virology, University of Padova, Padova, Italy.
Claudia Del Vecchio
Cristiano Salata
Michele Celestino
Marta Celegato
Heinrich Göttlinger
Giorgio Palù
Cristina Parolin
University of Padua · ITUniversity of Massachusetts Chan Medical School · US

Funding

Molecular Biology of HIV-Gag ProteinsR37AI029873 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GOTTLINGER, HEINRICH · 2004 to 2013
$5.1M
MOLECULAR BIOLOGY OF HIV GAG PROTEINSR01AI029873 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI GOTTLINGER, HEINRICH · 1990 to 2018
$3.7M
NIAID NIH HHS AI29873NIAID NIH HHS R01 AI029873NIAID NIH HHS R37 AI029873
6 · The paper itself

Abstract

RNA-enveloped viruses bud from infected cells by exploiting the multivesicular body (MVB) pathway. In this context, ubiquitination of structural viral proteins and their direct interaction with cellular factors involved in the MVB biogenesis through short proline rich regions, named late domains (L-domains), are crucial mechanisms. Here we report that, in contrast with the human immunodeficiency virus (HIV), the feline immunodeficiency virus (FIV), a non-primate lentivirus, is strictly dependent for its budding on a "PSAP"-type L-domain, mapping in the carboxy-terminal region of Gag, irrespective of a functional viral protease. Moreover, we provide evidence that FIV egress is related to Gag ubiquitination, that is, linked to the presence of an active L-domain. Finally, although FIV Gag does not contain a PPxY motif, we show that the Nedd4-2s ubiquitin ligase enhances FIV Gag ubiquitination and it is capable to rescue viral mutants lacking a functional L-domain. In conclusion, our data bring to light peculiar aspects of FIV egress, but we also demonstrate that a non-primate lentivirus shares with HIV-1 a novel mechanism of connection to the cellular budding machinery.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsCatsCell LineEndosomal Sorting Complexes Required for TransportGene Products, gagGenes, gagHIV-1HumansImmunodeficiency Virus, FelineMutagenesis, Site-DirectedMutationNedd4 Ubiquitin Protein LigasesProtein Processing, Post-TranslationalProtein Structure, TertiaryEndosomal Sorting Complexes Required for TransportGene Products, gagNedd4 protein, humanNedd4 Ubiquitin Protein LigasesUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID18792916
PMCPMC2593634
OpenAlexW1970114415

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.