Evidence map›Paper›PMID 10066836›Full record

ReviewMicrobiology and molecular biology reviews : MMBR1999

Surface proteins of gram-positive bacteria and mechanisms of their targeting to the cell wall envelope.

W W Navarre, O Schneewind

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 482 papers.

0numbers the graph read from it
0cells of the map it votes in
482citing papers in PubMed
69.3field-weighted citation impact, top 1% 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

482 citing papers in PubMed, 1,376 citations in OpenAlex.

  1. Article
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  7. ImmunogenicmSphere · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. A novel polysaccharide in the envelope ofJournal of bacteriology · 2025
    Article
  19. Peptidoglycan derived fromFrontiers in immunology · 2025
    Article
  20. Article

422 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

2 authors at 1 institution in 1 country.

W W NavarreDepartment of Microbiology & Immunology, UCLA School of Medicine, Los Angeles, California 90095, USA.
O Schneewind
University of California, Los Angeles · US

Funding

UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Surface Proteins of Gram-Positive BacteriaR01AI038897 · NIAID · UNIVERSITY OF CHICAGO · PI MISSIAKAS, DOMINIQUE M. · 1996 to 2024
$8.9M
CELL WALL ANCHORING OF STAPHYLOCOCCAL PROTEIN AR29AI033985 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SCHNEEWIND, OLAF · 1993 to 1997
–
NIAID NIH HHS AI33985NIAID NIH HHS AI38897NIAID NIH HHS R01 AI038897NIGMS NIH HHS GM 07185-22NIGMS NIH HHS T32 GM007185
6 · The paper itself

Abstract

The cell wall envelope of gram-positive bacteria is a macromolecular, exoskeletal organelle that is assembled and turned over at designated sites. The cell wall also functions as a surface organelle that allows gram-positive pathogens to interact with their environment, in particular the tissues of the infected host. All of these functions require that surface proteins and enzymes be properly targeted to the cell wall envelope. Two basic mechanisms, cell wall sorting and targeting, have been identified. Cell well sorting is the covalent attachment of surface proteins to the peptidoglycan via a C-terminal sorting signal that contains a consensus LPXTG sequence. More than 100 proteins that possess cell wall-sorting signals, including the M proteins of Streptococcus pyogenes, protein A of Staphylococcus aureus, and several internalins of Listeria monocytogenes, have been identified. Cell wall targeting involves the noncovalent attachment of proteins to the cell surface via specialized binding domains. Several of these wall-binding domains appear to interact with secondary wall polymers that are associated with the peptidoglycan, for example teichoic acids and polysaccharides. Proteins that are targeted to the cell surface include muralytic enzymes such as autolysins, lysostaphin, and phage lytic enzymes. Other examples for targeted proteins are the surface S-layer proteins of bacilli and clostridia, as well as virulence factors required for the pathogenesis of L. monocytogenes (internalin B) and Streptococcus pneumoniae (PspA) infections. In this review we describe the mechanisms for both sorting and targeting of proteins to the envelope of gram-positive bacteria and review the functions of known surface proteins.

Indexed as

Amino Acid SequenceBacterial Outer Membrane ProteinsBacterial ProteinsGram-Positive BacteriaLysostaphinMolecular Sequence DataN-Acetylmuramoyl-L-alanine AmidaseOpen Reading FramesOrganellesPeptidoglycanPolysaccharidesStaphylococcal Protein ATeichoic AcidsVirulenceBacterial Outer Membrane ProteinsBacterial Proteinsinternalin protein, BacteriaLysostaphinN-Acetylmuramoyl-L-alanine AmidasePeptidoglycanpneumococcal surface protein APolysaccharidesStaphylococcal Protein ATeichoic Acids

Identifiers

PMID10066836
PMCPMC98962
OpenAlexW2146052711

What OpenQuestion holds

Texttitle and abstract
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.