Evidence map›Paper›PMID 22026821›Full record

ReviewMolecular microbiology2011

Sortase enzymes in Gram-positive bacteria.

Thomas Spirig, Ethan M Weiner, Robert T Clubb

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.

0numbers the graph read from it
0cells of the map it votes in
160citing papers in PubMed
6.3field-weighted citation impact, top 3% 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

160 citing papers in PubMed, 323 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Integrative Analysis ofDentistry journal · 2026
    Article
  7. Article
  8. Functional Characterization of a Putative Sortase FA1364 inInternational journal of molecular sciences · 2026
    Article
  9. Microorganisms · 2026
    Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Amino acid variants at the P94 position inbioRxiv : the preprint server for biology · 2026
    Article
  15. A Putative Interaction between the Transmembrane Domains ofThe journal of physical chemistry. B · 2025
    Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

100 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 2 countries.

Thomas SpirigDepartment of Chemistry and Biochemistry, University of California, Los Angeles, Los Angeles, CA 90095, USA.
Ethan M Weiner
Robert T Clubb
University of California, Los Angeles · USGenomics (United Kingdom) · GB

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Cell Surface Protein Anchoring in Gram-Positive BacteriaR01AI052217 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Robert Thompson Clubb · 2002 to 2026
$8.5M
NIAID NIH HHS AI52217NIAID NIH HHS R01 AI052217NIGMS NIH HHS GM07185NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

In Gram-positive bacteria proteins are displayed on the cell surface using sortase enzymes. These cysteine transpeptidases join proteins bearing an appropriate sorting signal to strategically positioned amino groups on the cell surface. Working alone, or in concert with other enzymes, sortases either attach proteins to the cross-bridge peptide of the cell wall or they link proteins together to form pili. Because surface proteins play a fundamental role in microbial physiology and are frequently virulence factors, sortase enzymes have been intensely studied since their discovery a little more than a decade ago. Based on their primary sequences and functions sortases can be partitioned into distinct families called class A to F enzymes. Most bacteria elaborate their surfaces using more than one type of sortase that function non-redundantly by recognizing unique sorting signals within their protein substrates. Here we review what is known about the functions of these enzymes and the molecular basis of catalysis. Particular emphasis is placed on 'pilin' specific class C sortases that construct structurally complex pili. Exciting new data have revealed that these enzymes are amazingly promiscuous in the substrates that they can employ and that there is a startling degree of diversity in their mechanism of action. We also review recent data that suggest that sortases are targeted to specific sites on the cell surface where they work with other sortases and accessory factors to properly function.

Indexed as

AminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesFimbriae, BacterialFimbriae ProteinsGram-Positive BacteriaMembrane ProteinsModels, BiologicalModels, ChemicalSubstrate SpecificityAminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesFimbriae ProteinsMembrane Proteins

Identifiers

PMID22026821
PMCPMC3590066
OpenAlexW1929520690

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.