Evidence map›Paper›PMID 24002364›Full record

ArticleMolecular & cellular proteomics : MCP2013

Surface proteome analysis of a natural isolate of Lactococcus lactis reveals the presence of pili able to bind human intestinal epithelial cells.

Mickael Meyrand, Alain Guillot, Mélodie Goin, Sylviane Furlan, Julija Armalyte, Saulius Kulakauskas, Naima G Cortes-Perez, Ginette Thomas, Sophie Chat, Christine Péchoux and 5 more

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. 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
3.4field-weighted citation impact, top 7% 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

28 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Health-Promoting Nature ofFrontiers in microbiology · 2022
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Genetics of Lactococci.Microbiology spectrum · 2019
    Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Surface Proteins ofFrontiers in microbiology · 2017
    Review
  18. Cell Surface Properties ofFrontiers in microbiology · 2017
    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

15 authors at 3 institutions in 3 countries.

Mickael MeyrandINRA, UMR1319 Micalis, F-78350 Jouy-en-Josas, France;
Alain Guillot
Mélodie Goin
Sylviane Furlan
Julija Armalyte
Saulius Kulakauskas
Naima G Cortes-Perez
Ginette Thomas
Sophie Chat
Christine Péchoux
Vincent Dupres
Pascal Hols
Yves F Dufrêne
Germain Trugnan
Marie-Pierre Chapot-Chartier
Institut National de la Recherche Agronomique · MAUCLouvain · BEInserm · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Surface proteins of Gram-positive bacteria play crucial roles in bacterial adhesion to host tissues. Regarding commensal or probiotic bacteria, adhesion to intestinal mucosa may promote their persistence in the gastro-intestinal tract and their beneficial effects to the host. In this study, seven Lactococcus lactis strains exhibiting variable surface physico-chemical properties were compared for their adhesion to Caco-2 intestinal epithelial cells. In this test, only one vegetal isolate TIL448 expressed a high-adhesion phenotype. A nonadhesive derivative was obtained by plasmid curing from TIL448, indicating that the adhesion determinants were plasmid-encoded. Surface-exposed proteins in TIL448 were analyzed by a proteomic approach consisting in shaving of the bacterial surface with trypsin and analysis of the released peptides by LC-MS/MS. As the TIL448 complete genome sequence was not available, the tryptic peptides were identified by a mass matching approach against a database including all Lactococcus protein sequences and the sequences deduced from partial DNA sequences of the TIL448 plasmids. Two surface proteins, encoded by plasmids in TIL448, were identified as candidate adhesins, the first one displaying pilin characteristics and the second one containing two mucus-binding domains. Inactivation of the pilin gene abolished adhesion to Caco-2 cells whereas inactivation of the mucus-binding protein gene had no effect on adhesion. The pilin gene is located inside a cluster of four genes encoding two other pilin-like proteins and one class-C sortase. Synthesis of pili was confirmed by immunoblotting detection of high molecular weight forms of pilins associated to the cell wall as well as by electron and atomic force microscopy observations. As a conclusion, surface proteome analysis allowed us to detect pilins at the surface of L. lactis TIL448. Moreover we showed that pili appendages are formed and involved in adhesion to Caco-2 intestinal epithelial cells.

Indexed as

Gene Expression Regulation, BacterialAdhesins, BacterialAmino Acid SequenceAminoacyltransferasesBacterial AdhesionBacterial ProteinsCaco-2 CellsChromatography, LiquidCysteine EndopeptidasesFimbriae, BacterialFimbriae ProteinsHumansIntestinesLactococcus lactisMicroscopy, ElectronMolecular Sequence AnnotationAdhesins, BacterialAminoacyltransferasesBacterial ProteinsCysteine EndopeptidasesFimbriae ProteinsPeptide FragmentsProteomesortase CTrypsin

Identifiers

PMID24002364
PMCPMC3861735
OpenAlexW2141972758

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.