Evidence map›Paper›PMID 12183530›Full record

ArticleInfection and immunity2002

Involvement of Lsp, a member of the LraI-lipoprotein family in Streptococcus pyogenes, in eukaryotic cell adhesion and internalization.

Andrea Elsner, Bernd Kreikemeyer, Andrea Braun-Kiewnick, Barbara Spellerberg, Bettina A Buttaro, Andreas Podbielski

Abstract read
In one paragraph

Article in Infection and immunity, 2002. 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
5.4field-weighted citation impact, top 5% 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, 74 citations in OpenAlex.

  1. Interplay between group AMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Intracellular Invasion byMicrobiology spectrum · 2019
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Lipoproteins of bacterial pathogens.Infection and immunity · 2011
    Review
  13. Article
  14. Streptococcus adherence and colonization.Microbiology and molecular biology reviews : MMBR · 2009
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Purification, crystallization and preliminary crystallographic analysis of Streptococcus pyogenes laminin-binding protein Lbp.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008
    Article
  20. Group A streptococcus and its antibiotic resistance.Acta otorhinolaryngologica Italica : organo ufficiale della Societa italiana di otorinolaringologia e chirurgia cervico-facciale · 2007
    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

6 authors.

Andrea ElsnerDepartment of Medical Microbiology and Hygiene, University Hospital, D-18057 Rostock, Germany.
Bernd Kreikemeyer
Andrea Braun-Kiewnick
Barbara Spellerberg
Bettina A Buttaro
Andreas Podbielski

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Three open reading frames (ORFs) were identified by a genome walking strategy in the genomes of serotype M49 group A streptococcal (GAS) strains CS101 and 591. These ORFs were located between the mga core regulon and the dipeptide permease operon. The deduced amino acid (aa) sequences contained signature sequences indicative of a lipoprotein (306 aa), an intracellular protein (823 aa), and a secreted peptide (66 aa), respectively. ORF1 (named Lsp for lipoprotein of Streptococcus pyogenes) and ORF2 exhibited a high degree of homology to the lmb/ORF2 genes of S. agalactiae (B. Spellerberg et al., Infect. Immun. 67:871-878, 1999). The three ORFs were found to be present in each of the 27 GAS serotype strains tested. Transcription analysis revealed a polycistronic lsp/ORF2 and a monocistronic ORF3 message that were detected primarily at the transition from exponential to stationary growth phase. lsp and ORF2 mutants, ORF2- and ORF3-luciferase reporter fusions, and antiserum against recombinant Lsp were produced to examine the biological role of these genes. Although high Zn(2+) and Cu(2+) ion concentrations decreased lsp operon expression, Lsp did not transport divalent cations as described for other LraI-type operons. The lsp mutant had reduced fibronectin binding. Although no direct binding of Lsp to fibronectin could be demonstrated, the lsp mutant showed decreased transcription of prtF2 encoding the fibronectin-binding protein F2. Both the lsp and ORF2 mutants showed decreased laminin binding. Adherence to and internalization into A549 epithelial cells of both mutants was reduced without a detectable effect on eukaryotic cell viability. The transcription of a number of virulence factors was altered in the lsp mutants and ORF2 mutants. The changes in laminin binding and eukaryotic cell internalization could be explained by changes in transcription of speB (cysteine protease) and/or the global regulators mga, csrRS, and nra.

Indexed as

Bacterial ProteinsBase SequenceCations, DivalentCell AdhesionCell LineDNA, BacterialGenes, BacterialHumansIn Vitro TechniquesLamininLipoproteinsMolecular Sequence DataMutationOpen Reading FramesRNA, BacterialRNA, MessengerBacterial ProteinsCations, DivalentDNA, BacterialLamininLipoproteinsRNA, BacterialRNA, Messenger

Identifiers

PMID12183530
PMCPMC128222
OpenAlexW2062794235

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.