Evidence map›Paper›PMID 29540600›Full record

ArticleJournal of virology2018

Baculovirus AC102 Is a Nucleocapsid Protein That Is Crucial for Nuclear Actin Polymerization and Nucleocapsid Morphogenesis.

Susan E Hepp, Gina M Borgo, Simina Ticau, Taro Ohkawa, Matthew D Welch

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Nuclear Cytoskeleton in Virus Infection.International journal of molecular sciences · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. 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

5 authors at 1 institution in 1 country.

Susan E HeppGraduate Group in Microbiology, University of California, Berkeley, California, USA.
Gina M BorgoGraduate Group in Infectious Diseases and Immunity, University of California, Berkeley, California, USA.
Simina TicauDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
Taro OhkawaDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA.
Matthew D WelchDepartment of Molecular and Cell Biology, University of California, Berkeley, California, USA welch@berkeley.edu.
University of California, Berkeley · US

Funding

FUNCTION &REGULATION OF THE HUMAN ARP2/3 COMPLEXR01GM059609 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI WELCH, MATTHEW D · 1999 to 2017
$5.1M
Microbial mobilization of the actin cytoskeletonR35GM127108 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI Matthew D Welch · 2018 to 2026
$4.0M
Automated High-Throughput, High-Content Confocal/Wide-Field Microscope SystemS10OD021828 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI WEST, MARY · 2017 to 2017
$1.0M
NIGMS NIH HHS R01 GM059609NIGMS NIH HHS R35 GM127108NIH HHS S10 OD021828
6 · The paper itself

Abstract

The baculovirus Autographa californica multiple nucleopolyhedrovirus (AcMNPV), the type species of alphabaculoviruses, is an enveloped DNA virus that infects lepidopteran insects and is commonly known as a vector for protein expression and cell transduction. AcMNPV belongs to a diverse group of viral and bacterial pathogens that target the host cell actin cytoskeleton during infection. AcMNPV is unusual, however, in that it absolutely requires actin translocation into the nucleus early in infection and actin polymerization within the nucleus late in infection coincident with viral replication. Of the six viral factors that are sufficient, when coexpressed, to induce the nuclear localization of actin, only AC102 is essential for viral replication and the nuclear accumulation of actin. We therefore sought to better understand the role of AC102 in actin mobilization in the nucleus early and late in infection. Although AC102 was proposed to function early in infection, we found that AC102 is predominantly expressed as a late protein. In addition, we observed that AC102 is required for F-actin assembly in the nucleus during late infection, as well as for proper formation of viral replication structures and nucleocapsid morphogenesis. Finally, we found that AC102 is a nucleocapsid protein and a newly recognized member of a complex consisting of the viral proteins EC27, C42, and the actin polymerization protein P78/83. Taken together, our findings suggest that AC102 is necessary for nucleocapsid morphogenesis and actin assembly during late infection through its role as a component of the P78/83-C42-EC27-AC102 protein complex.

Indexed as

Actin CytoskeletonActinsAnimalsCell LineCell NucleusNucleocapsid ProteinsNucleopolyhedrovirusesPolymerizationProtein BiosynthesisSf9 CellsSpodopteraVirus ReplicationActinsNucleocapsid Proteinsactinbaculovirus

Identifiers

PMID29540600
PMCPMC5952165
OpenAlexW2950665405

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.