Evidence map›Paper›PMID 26912609›Full record

ArticleJournal of virology2016

Crystal Structure of the Oligomeric Form of Lassa Virus Matrix Protein Z.

Kathryn M Hastie, Michelle Zandonatti, Tong Liu, Sheng Li, Virgil L Woods, Erica Ollmann Saphire

Abstract read
In one paragraph

Article in Journal of virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Architectural organization andJournal of virology · 2024
    Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Structural and molecular biology of Sabiá virus.Experimental biology and medicine (Maywood, N.J.) · 2023
    Review
  10. Article
  11. Lassa Virus Structural Biology and Replication.Current topics in microbiology and immunology · 2023
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Article
  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

6 authors.

Kathryn M HastieDepartment of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
Michelle ZandonattiDepartment of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA.
Tong LiuDepartment of Medicine, University of California-San Diego, La Jolla, California, USA.
Sheng LiDepartment of Medicine, University of California-San Diego, La Jolla, California, USA.
Virgil L WoodsDepartment of Medicine, University of California-San Diego, La Jolla, California, USA.
Erica Ollmann SaphireDepartment of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, California, USA The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California, USA erica@scripps.edu.

Funding

NIAID NIH HHS HHSN272200900049CPHS HHS HHSN272200900049C
6 · The paper itself

Abstract

unlabelledThe arenavirus matrix protein Z is highly multifunctional and occurs in both monomeric and oligomeric forms. The crystal structure of a dodecamer of Z from Lassa virus, presented here, illustrates a ring-like structure with a highly basic center. Mutagenesis demonstrates that the dimeric interface within the dodecamer and a Lys-Trp-Lys triad at the center of the ring are important for oligomerization. This structure provides an additional template to explore the many functions of Z. IMPORTANCE: The arenavirus Lassa virus causes hundreds of thousands of infections each year, many of which develop into fatal hemorrhagic fever. The arenavirus matrix protein Z is multifunctional, with at least four distinct roles. Z exists in both monomeric and oligomeric forms, each of which likely serves a specific function in the viral life cycle. Here we present the dodecameric form of Lassa virus Z and demonstrate that Z forms a "wreath" with a highly basic center. This structure and that of monomeric Z now provide a pair of critical templates by which the multiple roles of Z in the viral life cycle may be interpreted.

Indexed as

Lassa virusModels, MolecularProtein ConformationProtein MultimerizationCarrier ProteinsCrystallography, X-RayMass SpectrometryNuclear Magnetic Resonance, BiomolecularRecombinant Fusion ProteinsRNA-Binding ProteinsStructure-Activity RelationshipViral Matrix ProteinsCarrier Proteinsprotein Z, Lassa virusRecombinant Fusion ProteinsRNA-Binding ProteinsViral Matrix Proteins

Identifiers

PMID26912609
PMCPMC4836352

What OpenQuestion holds

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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.