Evidence map›Paper›PMID 21454677›Full record

ArticleThe Journal of biological chemistry2011

Functional and structural characterization of polysaccharide co-polymerase proteins required for polymer export in ATP-binding cassette transporter-dependent capsule biosynthesis pathways.

Kane Larue, Robert C Ford, Lisa M Willis, Chris Whitfield

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Periplasmic depolymerase provides insight into ABC transporter-dependent secretion of bacterial capsular polysaccharides.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  10. Article
  11. Regulation of capsule in Neisseria meningitidis.Critical reviews in microbiology · 2016
    Review
  12. Unique lipid anchor attaches Vi antigen capsule to the surface of Salmonella enterica serovar Typhi.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  13. Quaternary structure of WzzB and WzzE polysaccharide copolymerases.Protein science : a publication of the Protein Society · 2015
    Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. KpsC and KpsS are retaining 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) transferases involved in synthesis of bacterial capsules.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

4 authors.

Kane LarueDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario, Canada N1G 2W1.
Robert C Ford
Lisa M Willis
Chris Whitfield

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Neisseria meningitidis serogroup B and Escherichia coli K1 bacteria produce a capsular polysaccharide (CPS) that is composed of α2,8-linked polysialic acid (PSA). Biosynthesis of PSA in these bacteria occurs via an ABC (ATP-binding cassette) transporter-dependent pathway. In N. meningitidis, export of PSA to the surface of the bacterium requires two proteins that form an ABC transporter (CtrC and CtrD) and two additional proteins, CtrA and CtrB, that are proposed to form a cell envelope-spanning export complex. CtrA is a member of the outer membrane polysaccharide export (OPX) family of proteins, which are proposed to form a pore to mediate export of CPSs across the outer membrane. CtrB is an inner membrane protein belonging to the polysaccharide co-polymerase (PCP) family. PCP proteins involved in other bacterial polysaccharide assembly systems form structures that extend into the periplasm from the inner membrane. There is currently no structural information available for PCP or OPX proteins involved in an ABC transporter-dependent CPS biosynthesis pathway to support their proposed roles in polysaccharide export. Here, we report cryo-EM images of purified CtrB reconstituted into lipid bilayers. These images contained molecular top and side views of CtrB and showed that it formed a conical oligomer that extended ∼125 Å from the membrane. This structure is consistent with CtrB functioning as a component of an envelope-spanning complex. Cross-complementation of CtrA and CtrB in E. coli mutants with defects in genes encoding the corresponding PCP and OPX proteins show that PCP-OPX pairs require interactions with their cognate partners to export polysaccharide. These experiments add further support for the model of an ABC transporter-PCP-OPX multiprotein complex that functions to export CPS across the cell envelope.

Indexed as

Gene Expression Regulation, BacterialAdenosine TriphosphateAmino Acid SequenceATP-Binding Cassette TransportersBiological TransportCryoelectron MicroscopyEscherichia coliGenetic Complementation TestLipid BilayersModels, GeneticMolecular Sequence DataNeisseria meningitidisPolymersPolysaccharidesSequence Homology, Amino AcidAdenosine TriphosphateATP-Binding Cassette TransportersLipid BilayersPolymersPolysaccharides

Identifiers

PMID21454677
PMCPMC3089508

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.