دورية أكاديمية
Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50.
| العنوان: | Variable carbohydrate modifications to the catalytic chains of the RgpA and RgpB proteases of Porphyromonas gingivalis W50. |
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| المؤلفون: | Curtis MA; MRC Molecular Pathogenesis Group, Department of Oral Microbiology, St. Bartholomew's and the Royal London School of Medicine and Dentistry, Queen Mary and Westfield College, London E1 2AA, United Kingdom. M.A.Curtis@mds.qmw.ac.uk, Thickett A, Slaney JM, Rangarajan M, Aduse-Opoku J, Shepherd P, Paramonov N, Hounsell EF |
| المصدر: | Infection and immunity [Infect Immun] 1999 Aug; Vol. 67 (8), pp. 3816-23. |
| نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
| اللغة: | English |
| بيانات الدورية: | Publisher: American Society For Microbiology Country of Publication: United States NLM ID: 0246127 Publication Model: Print Cited Medium: Print ISSN: 0019-9567 (Print) Linking ISSN: 00199567 NLM ISO Abbreviation: Infect Immun Subsets: MEDLINE |
| أسماء مطبوعة: | Publication: Washington, DC : American Society For Microbiology Original Publication: [Bethesda, Md.] American Society for Microbiology. |
| مواضيع طبية MeSH: | Carbohydrates/*chemistry , Cysteine Endopeptidases/*chemistry , Endopeptidases/*chemistry , Hemagglutinins/*chemistry , Porphyromonas gingivalis/*enzymology, Adhesins, Bacterial ; Animals ; Antibodies, Monoclonal/immunology ; Catalytic Domain ; Cysteine Endopeptidases/immunology ; Endopeptidases/immunology ; Female ; Gingipain Cysteine Endopeptidases ; Glycosylation ; Hemagglutinins/immunology ; Lipopolysaccharides/chemistry ; Mice ; Mice, Inbred BALB C |
| مستخلص: | Proteases of Porphyromonas gingivalis are considered to be important virulence determinants of this periodontal bacterium. Several biochemical isoforms of arginine-specific proteases are derived from rgpA and rgpB. HRgpA is a heterodimer composed of the catalytic alpha chain noncovalently associated with a beta adhesin chain derived from the C terminus of the initial full-length translation product. The catalytic alpha chain is also present as a monomer (RgpA) either free in solution or associated with membranes. rgpB lacks the coding region for the adhesin domain present in rgpA and yields only monomeric forms (RgpB) which again may be soluble or membrane associated. In this study, the catalytic chains of this unusual group of enzymes are shown to be differentially modified by the posttranslational addition of carbohydrate. A monoclonal antibody (MAb 1B5) raised to the monomeric RgpA did not react with the corresponding recombinant RgpA alpha chain expressed in Escherichia coli but was immunoreactive with P. gingivalis lipopolysaccharide. MAb 1B5 also reacted with the membrane-associated forms of RgpA and RgpB but not with the heterodimeric HRgpA and the soluble form of RgpB. RgpA treated with denaturants was capable of binding to MAb 1B5 whereas treatment with periodate abolished this binding, suggesting the presence of carbohydrate residues within the epitope. Chemical deglycosylation abolished immunoreactivity with MAb 1B5 and caused a approximately 30% reduction in the size of the membrane-associated enzymes. Monosaccharide analysis of HRgpA and RgpA demonstrated 2.1 and 14.4%, respectively, carbohydrate by weight of protein. Furthermore, distinct differences were detected in their monosaccharide compositions, indicating that these protease isoforms are modified not only to different extents but also with different sugars. The variable nature of these additions may have a significant effect on the structure, stability, and immune recognition of these protease glycoproteins. |
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| المشرفين على المادة: | 0 (Adhesins, Bacterial) 0 (Antibodies, Monoclonal) 0 (Carbohydrates) 0 (Gingipain Cysteine Endopeptidases) 0 (Hemagglutinins) 0 (Lipopolysaccharides) EC 3.4.- (Endopeptidases) EC 3.4.22.- (Cysteine Endopeptidases) EC 3.4.99.- (arginine protease) |
| تواريخ الأحداث: | Date Created: 19990723 Date Completed: 19990812 Latest Revision: 20221006 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC96659 |
| DOI: | 10.1128/IAI.67.8.3816-3823.1999 |
| PMID: | 10417143 |
| قاعدة البيانات: | MEDLINE |
| تدمد: | 0019-9567 |
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| DOI: | 10.1128/IAI.67.8.3816-3823.1999 |