Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-6-29
pubmed:abstractText
Porphyromonas gingivalis has been implicated as a major aetiological agent in certain forms of periodontal disease, P. gingivalis is a Gram-negative, asaccharolytic bacterium that obtains energy from the fermentation of amino acids derived from the hydrolysis of host protein. Virulence factors of this bacterium include the capsule, fimbrial adhesins, cytotoxins and extracellular hydrolytic enzymes. A 43 kDa fimbrillin from P. gingivalis has been isolated and characterized. However, there is evidence that a second type of fimbria exists on the surface of P. gingivalis. A putative P. gingivalis fimbrial protein from a membrane preparation has been isolated and identified. This protein was shown to be reactive with sera from patients harbouring P. gingivalis. A 28 kDa protein fragment was purified by anion exchange, gel filtration and reversed-phase chromatography. N-terminal sequence analysis of the 28 kDa protein fragment revealed homology to the fimbrial precursor protein of Dichelobacter nodosus. A peptide corresponding to the N-terminal 26 amino acyl residues of the 28 kDa protein fragment was synthesized and used to raise antibodies to the protein. Western blot analysis after SDS-PAGE of a P. gingivalis membrane preparation using the antibodies raised to the synthetic peptide detected three proteins of 36, 41 and 67 kDa. When protease inhibitors were not included in the extraction procedure only the 36 and 41 kDa bands were detected. It would appear, therefore, that the intact protein has an M(r) of 67 kDa and that the 28, 36 and 41 kDa bands represent protein fragments produced by endogenous proteolytic activity. Based on sequence homology, the 67 kDa protein is possibly a sub-unit of a second P. gingivalis fimbrial type or a surface receptor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adhesins, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Bacterial, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Capsules, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cytotoxins, http://linkedlifedata.com/resource/pubmed/chemical/Fimbriae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments, http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Dodecyl Sulfate, http://linkedlifedata.com/resource/pubmed/chemical/fimbrillin
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0045-0421
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
99-104
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9612983-Adhesins, Bacterial, pubmed-meshheading:9612983-Animals, pubmed-meshheading:9612983-Antibodies, Bacterial, pubmed-meshheading:9612983-Antigens, Bacterial, pubmed-meshheading:9612983-Bacterial Capsules, pubmed-meshheading:9612983-Bacterial Outer Membrane Proteins, pubmed-meshheading:9612983-Bacterial Proteins, pubmed-meshheading:9612983-Bacteroides, pubmed-meshheading:9612983-Blotting, Western, pubmed-meshheading:9612983-Chromatography, Gel, pubmed-meshheading:9612983-Chromatography, Ion Exchange, pubmed-meshheading:9612983-Cytotoxins, pubmed-meshheading:9612983-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:9612983-Fimbriae, Bacterial, pubmed-meshheading:9612983-Fimbriae Proteins, pubmed-meshheading:9612983-Humans, pubmed-meshheading:9612983-Hydrolases, pubmed-meshheading:9612983-Molecular Weight, pubmed-meshheading:9612983-Peptide Fragments, pubmed-meshheading:9612983-Periodontal Diseases, pubmed-meshheading:9612983-Porphyromonas gingivalis, pubmed-meshheading:9612983-Protease Inhibitors, pubmed-meshheading:9612983-Protein Precursors, pubmed-meshheading:9612983-Sequence Homology, Amino Acid, pubmed-meshheading:9612983-Sodium Dodecyl Sulfate, pubmed-meshheading:9612983-Virulence
pubmed:year
1998
pubmed:articleTitle
Purification and characterization of a putative fimbrial protein/receptor of Porphyromonas gingivalis.
pubmed:affiliation
Biochemistry and Molecular Biology Unit, School of Dental Science, University of Melbourne.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't