Evidence map›Paper›PMID 22072775›Full record

ArticleJournal of virology2012

Cellular VPS4 is required for efficient entry and egress of budded virions of Autographa californica multiple nucleopolyhedrovirus.

Zhaofei Li, Gary W Blissard

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

19 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  7. The Role of Exosome and the ESCRT Pathway on Enveloped Virus Infection.International journal of molecular sciences · 2021
    Review
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  18. Functional interplay between a virus and the ESCRT machinery in archaea.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. 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 1 institution in 1 country.

Zhaofei LiBoyce Thompson Institute at Cornell University, Ithaca, New York, USA.
Gary W Blissard
Cornell University · US

Funding

FUNCTION OF THE BACULOVIRUS MEMBRANE FUSION PROTEINR01AI033657 · NIAID · BOYCE THOMPSON INST FOR PLANT RESEARCH · PI BLISSARD, GARY W · 1993 to 2009
$1.6M
Baculovirus envelope proteins and insect cellsR21AI033657 · NIAID · BOYCE THOMPSON INST FOR PLANT RESEARCH · PI BLISSARD, GARY W · 2004 to 2004
$189k
NIAID NIH HHS AI33657NIAID NIH HHS R01 AI033657NIAID NIH HHS R21 AI033657
6 · The paper itself

Abstract

Membrane budding is essential for the egress of many enveloped viruses, and this process shares similarities with the biogenesis of multivesicular bodies (MVBs). In eukaryotic cells, the budding of intraluminal vesicles (IVLs) is mediated by the endosomal sorting complex required for transport (ESCRT) machinery and some viruses require ESCRT machinery components or functions to bud from host cells. Baculoviruses, such as Autographa californica multiple nucleopolyhedrovirus (AcMNPV), enter host cells by clathrin-mediated endocytosis. Viral DNA replication and nucleocapsid assembly occur within the nucleus. Some progeny nucleocapsids are subsequently trafficked to, and bud from, the plasma membrane, forming budded virions (BV). To determine whether the host ESCRT machinery is important or necessary for AcMNPV replication, we cloned a cDNA of Spodoptera frugiperda VPS4, a key regulator for disassembly and recycling of ESCRT III. We then examined viral infection and budding in the presence of wild-type (WT) or dominant negative (DN) forms of VPS4. First, we used a viral complementation system, in combination with fluorescent tags, to examine the effects of transiently expressed WT or DN VPS4 on viral entry. We found that dominant negative VPS4 substantially inhibited virus entry. Entering virus was observed within aberrant compartments containing the DN VPS4 protein. We next used recombinant bacmids expressing WT or DN VPS4 proteins to examine virus egress. We found that production of infectious AcMNPV BV was substantially reduced by expression of DN VPS4 but not by WT VPS4. Together, these results indicate that a functional VPS4 is necessary for efficient AcMNPV BV entry into, and egress from, insect cells.

Indexed as

Virus InternalizationVirus ReleaseAmino Acid SequenceAnimalsEndosomal Sorting Complexes Required for TransportInsect ProteinsMolecular Sequence DataNucleopolyhedrovirusesSequence AlignmentSpodopteraVirionVirus ReplicationEndosomal Sorting Complexes Required for TransportInsect Proteins

Identifiers

PMID22072775
PMCPMC3255925
OpenAlexW2109900607

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.