Evidence map›Paper›PMID 19228054›Full record

ArticleJournal of proteome research2009

S-layer, surface-accessible, and concanavalin A binding proteins of Methanosarcina acetivorans and Methanosarcina mazei.

Deborah R Francoleon, Pinmanee Boontheung, Yanan Yang, UnMi Kin, A Jimmy Ytterberg, Patricia A Denny, Paul C Denny, Joseph A Loo, Robert P Gunsalus, Rachel R Ogorzalek Loo

Open access · greenAbstract read
In one paragraph

Article in Journal of proteome research, 2009. 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
1.8field-weighted citation impact, top 15% 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. Cell surface differences within the genusJournal of bacteriology · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Emerging facets of prokaryotic glycosylation.FEMS microbiology reviews · 2017
    Review
  7. Review
  8. Article
  9. Article
  10. Article
  11. N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Microbiology and molecular biology reviews : MMBR · 2014
    Review
  12. Review
  13. Effects of antimicrobial peptides on methanogenic archaea.Antimicrobial agents and chemotherapy · 2012
    Article
  14. Structure of the surface layer of the methanogenic archaean Methanosarcina acetivorans.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Shaping the archaeal cell envelope.Archaea (Vancouver, B.C.) · 2010
    Review
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

10 authors at 2 institutions in 1 country.

Deborah R FrancoleonDepartment of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA.
Pinmanee Boontheung
Yanan Yang
UnMi Kin
A Jimmy Ytterberg
Patricia A Denny
Paul C Denny
Joseph A Loo
Robert P Gunsalus
Rachel R Ogorzalek Loo
University of Southern California · USUniversity of California, Los Angeles · US

Funding

Impact of Non-canonical Decoding on the ProteomeR01GM085402 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A, OGORZALEK LOO, RACHEL R. · 2008 to 2011
$1.2M
Sortase A anchoring mechanismF31AI061886 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LEON-ROSSELL, DEBORAH · 2004 to 2007
$117k
NIAID NIH HHS 5 F31AI061886-02NIAID NIH HHS F31 AI061886NIGMS NIH HHS GM085402NIGMS NIH HHS R01 GM085402
6 · The paper itself

Abstract

The outermost cell envelope structure of many archaea and bacteria contains a proteinaceous lattice termed the surface layer or S-layer. It is typically composed of only one or two abundant, often posttranslationally modified proteins that self-assemble to form the highly organized arrays. Surprisingly, over 100 proteins were annotated to be S-layer components in the archaeal species Methanosarcina acetivorans C2A and Methanosarcina mazei Gö1, reflecting limitations of current predictions. An in vivo biotinylation methodology was devised to affinity tag surface-exposed proteins while overcoming unique challenges in working with these fragile organisms. Cells were adapted to growth under N2 fixing conditions, thus, minimizing free amines reactive to the NHS-label, and high pH media compatible with the acylation chemistry was used. A 3-phase separation procedure was employed to isolate intact, labeled cells from lysed-cell derived proteins. Streptavidin affinity enrichment followed by stringent wash conditions removed nonspecifically bound proteins. This methodology revealed S-layer proteins in M. acetivorans C2A and M. mazei Gö1 to be MA0829 and MM1976, respectively. Each was demonstrated to exist as multiple glycosylated forms using SDS-PAGE coupled with glycoprotein-specific staining, and by interaction with the lectin, Concanavalin A. A number of additional surface-exposed proteins and glycoproteins were identified and included all three subunits of the thermosome: the latter suggests that the chaperonin complex is both surface- and cytoplasmically localized. This approach provides an alternative strategy to study surface proteins in the archaea.

Indexed as

Archaeal ProteinsChromatography, High Pressure LiquidConcanavalin AGlycoproteinsMembrane GlycoproteinsMethanosarcinaProtein BindingProteomeReceptors, Concanavalin ATandem Mass SpectrometryArchaeal ProteinsConcanavalin AGlycoproteinsMembrane GlycoproteinsProteomeReceptors, Concanavalin AS-layer proteins

Identifiers

PMID19228054
PMCPMC2666069
OpenAlexW2081711857

What OpenQuestion holds

Textmetadata
LicenceTDM
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.