Evidence map›Paper›PMID 17329345›Full record

ArticleJournal of virology2007

Importance of the penultimate positive charge in mouse hepatitis coronavirus A59 membrane protein.

Sandhya Verma, Lisa A Lopez, Valerie Bednar, Brenda G Hogue

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Definition of the components required for selective packaging of coronavirus genomic RNA.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Coronavirus pathogenesis.Advances in virus research · 2011
    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

4 authors at 1 institution in 1 country.

Sandhya VermaBiodesign Institute, Center for Infectious Diseases and Vaccinology, PO Box 875401, Arizona State University, Tempe, AZ 85287-5401, USA.
Lisa A Lopez
Valerie Bednar
Brenda G Hogue
National Center for Infectious Diseases · US

Funding

Molecular Analysis of Coronavirus AssemblyR01AI053704 · NIAID · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI HOGUE, BRENDA G · 2003 to 2007
$1.3M
NIAID NIH HHS AI53704NIAID NIH HHS R01 AI053704
6 · The paper itself

Abstract

The coronavirus membrane (M) protein carboxy tail interacts with the nucleocapsid during virus assembly. Previous studies demonstrated that the two terminal residues are important, and the charged residue (R227) in the penultimate position in the mouse hepatitis coronavirus (MHV) A59 M protein was suggested to participate in intermolecular interactions with negative charges in the nucleocapsid (N) protein. To determine the significance of the positive charge at position 227, we substituted the arginine with lysine (K), aspartic acid (D), glutamic acid (E), or alanine (A) and studied these by reverse genetics in the context of a MHV full-length infectious clone. Viruses with wild-type phenotype were readily recovered with the K or A substitutions. In contrast, negative-charge substitutions were not tolerated as well. In all recovered R227D viruses the negative charge was replaced with heterologous residues resulting from apparent template switching during negative-strand synthesis of subgenomic RNA 7. An additional second-site compensatory V202I substitution was present in some viruses. Recovered R227E viruses had second-site changes within the M protein carboxy tail that were partially compensatory. Significantly, most of the second site changes in the R227E mutant viruses were previously shown to compensate for the removal of negative charges in the N protein. Our results strongly indicate that a positive charge is not absolutely required. It is clear that other regions within the tail must also be involved in helping mediate interactions between the M protein and the nucleocapsid.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsCell LineCoronavirus M ProteinsCoronavirus Nucleocapsid ProteinsCricetinaeMiceMicroscopy, ConfocalMicroscopy, FluorescenceMolecular Sequence DataMurine hepatitis virusMutagenesis, Site-DirectedNucleocapsid ProteinsProtein BindingSuppression, GeneticCoronavirus M ProteinsCoronavirus Nucleocapsid ProteinsNucleocapsid ProteinsViral Matrix Proteins

Identifiers

PMID17329345
PMCPMC1900233
OpenAlexW2126350576

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.