ArticleInfection and immunity1999
Streptococcus parasanguis pepO encodes an endopeptidase with structure and activity similar to those of enzymes that modulate peptide receptor signaling in eukaryotic cells.
Article in Infection and immunity, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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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.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- Identification and Characterization of Negative Regulators of Rgg1518 Quorum Sensing in Streptococcus pneumoniae.Journal of bacteriology · 2023Article
- Endopeptidase PepO Regulates the SpeB Cysteine Protease and Is Essential for the Virulence of Invasive M1T1 Streptococcus pyogenes.Journal of bacteriology · 2018Article
- PepO, a CovRS-controlled endopeptidase, disrupts Streptococcus pyogenes quorum sensing.Molecular microbiology · 2016Article
- The endothelin system has a significant role in the pathogenesis and progression of Mycobacterium tuberculosis infection.Infection and immunity · 2014Article
- Antivirulence genes: insights into pathogen evolution through gene loss.Infection and immunity · 2012Review
- Streptococcus pyogenes antigen I/II-family polypeptide AspA shows differential ligand-binding properties and mediates biofilm formation.Molecular microbiology · 2011Article
- Histochemical distribution of endothelin-converting enzyme subtypes in Podarcis sicula (Squamata, Lacertidae) tissues.Journal of anatomy · 2005Article
- Structure, evolutionary conservation, and functions of angiotensin- and endothelin-converting enzymes.International review of cytology · 2004Review
- Identification and characterization of Lactobacillus helveticus PepO2, an endopeptidase with post-proline specificity.Applied and environmental microbiology · 2003Article
- The divergently transcribed Streptococcus parasanguis virulence-associated fimA operon encoding an Mn(2+)-responsive metal transporter and pepO encoding a zinc metallopeptidase are not coordinately regulated.Infection and immunity · 2002Article
- Identification of a protein that inactivates the competence-stimulating peptide of Streptococcus pneumoniae.Journal of bacteriology · 2002Article
- Streptococcus parasanguis fimbria-associated adhesin fap1 is required for biofilm formation.Infection and immunity · 2001Article
- Characterization of a streptococcal endopeptidase with homology to human endothelin-converting enzyme.Infection and immunity · 2001Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Studies in our laboratory have identified two fimbria-associated adhesins, FimA and Fap1, of Streptococcus parasanguis FW213. In this study, we isolated and sequenced DNA fragments linked to fimA to determine if they contained additional factors associated with adherence, virulence, or survival in the host. An open reading frame just upstream and divergently transcribed from the fimA operon was identified and named pepO. Northern hybridization indicated that pepO is transcribed as a monocistronic message. pepO encodes a predicted 631-amino-acid protein with a molecular mass of approximately 70.6 kDa. PepO contains the essential motif HEXXH, typical of many zinc-dependent metalloproteases and metallopeptidases. PepO has significant sequence identity to mammalian metallopeptidases, including endothelin-converting enzyme, which converts a potent vasoconstrictor into its active form, and neutral endopeptidase (NEP), which is involved in terminating the activity of opioid peptides. The opioid peptide metenkephalin is a natural substrate of NEP. Cell extracts of FW213 cleaved metenkephalin at the same site as does NEP, while an extract from an insertionally inactivated pepO mutant did not. These results indicate that FW213 pepO encodes an enzyme with activity similar to that of known mammalian endopeptidases. Phylogenetic analysis of PepO and its homologues suggests lateral genetic exchange between bacteria and eukaryotes.
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