Evidence map›Paper›PMID 21646642›Full record

ArticleMolecular & cellular proteomics : MCP2011

Unraveling lactococcal phage baseplate assembly by mass spectrometry.

Dale A Shepherd, David Veesler, Julie Lichière, Alison E Ashcroft, Christian Cambillau

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. 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
4.6field-weighted citation impact, top 6% 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, 23 citations in OpenAlex.

  1. Article
  2. Review
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  9. Article
  10. Probing bunyavirus N protein oligomerisation using mass spectrometry.Rapid communications in mass spectrometry : RCM · 2014
    Article
  11. Review
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  16. Viral infection modulation and neutralization by camelid nanobodies.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. Article
  18. Review
  19. Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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 3 institutions in 2 countries.

Dale A ShepherdAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
David Veesler
Julie Lichière
Alison E Ashcroft
Christian Cambillau
Aix-Marseille Université · FRUniversity of Leeds · GBCentre National de la Recherche Scientifique · FR

Funding

Biotechnology and Biological Sciences Research Council BB/E012558/1Wellcome TrustWellcome Trust WT 075099/Z/04/Z
6 · The paper itself

Abstract

Bacteriophages belonging to the Caudovirales order possess a tail acting as a molecular machine used during infection to recognize the host and ensure high-efficiency genome delivery to the cell cytoplasm. They bear a large and sophisticated multiprotein organelle at their distal tail end, either a baseplate or a tail-tip, which is the control center for infectivity. We report here insights into the baseplate assembly pathways of two lactoccocal phages (p2 and TP901-1) using electrospray ionization-mass spectrometry. Based on our "block cloning" strategy we have expressed large complexes of their baseplates as well as several significant structural subcomplexes. Previous biophysical characterization using size-exclusion chromatography coupled with on-line light scattering and refractometry demonstrated that the overproduced recombinant proteins interact with each other to form large (up to 1.9 MDa) and stable assemblies. The structures of several of these complexes have been determined by x-ray diffraction or by electron microscopy. In this contribution, we demonstrate that electrospray ionization-mass spectrometry yields accurate mass measurements for the different baseplate complexes studied from which their stoichiometries can be discerned, and that the subspecies observed in the spectra provide valuable information on the assembly mechanisms of these large organelles.

Indexed as

Cloning, MolecularEscherichia coliLactococcus lactisMicroscopy, ElectronModels, MolecularMultiprotein ComplexesOpen Reading FramesPlasmidsProtein BindingRecombinant ProteinsSiphoviridaeSpectrometry, Mass, Electrospray IonizationViral Tail ProteinsVirus AssemblyMultiprotein ComplexesRecombinant ProteinsViral Tail Proteins

Identifiers

PMID21646642
PMCPMC3186816
OpenAlexW1978738180

What OpenQuestion holds

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LicenceCC BY-NC
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.