Total Record - 1

Print this rrecord

 
ProGlyProt ID
BU248
Organism Information
Organism Name
Porphyromonas (Bacteroides) gingivalis W50
Domain
Bacteria
Classification
Family: Porphyromonadaceae
Order: Bacteroidales
Class: Bacteroidia
Division or phylum: "Bacteroidetes"
 
 
Protein Information
Protein Name
mtRgpA
Subcellular Location
Extracellular
Function
Cysteine proteases cause the degradation of several physiologically important proteins, including collagens, fibrin and fibrinogen and fibronectin. They also account for deregulatory effects on several host systems and are therefore considered important virulence determinants. The adhesin domains of Arg-gingipains mediate the adherence of P. gingivalis to epithelial cells.
 
 
Glycosylation Status
Glycosylation Type
Information currently not available with us.
Technique(s) used for Glycosylation Detection
Biotin hydrazide labelling following periodate oxidation., chemical deglycosylation with TFMS and subsequent abolishment of immunoreactivity wth MAb 1B5 and MAb 7B4 after deglycosylation.
 
 
Literature
Reference(s)
1) Curtis, M.A., Thickett, A., Slaney, J.M., Rangarajan, M., Aduse-Opoku, J., Shepherd, P., Paramonov, N. and Hounsell, E.F. (1999) Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50. Infect Immun, 67, 3816-3823. [PubMed: 10417143]
Year of Identification
1999
 
 
Copyright @ 2011 IMTECH
This site is best viewed in Mozilla Firefox, Internet Explorer 6 and above at screen resolution of 1024 x 768 and above.