Characterization and detection of the 40 kDa fimbrial subunit of Bacteroides fragilis BE1.
The amino acid composition and amino-terminal amino acid sequence of the 40 kDa fimbrial subunit of Bacteroides fragilis were determined. No similarity with other known fimbrial subunits or protein sequences was found. The isoelectric point of the fimbriae was determined to be 3.8. The acidic nature of these fimbriae is in agreement with the amino acid composition of the fimbrial subunit. An IgM monoclonal antibody, raised against the denaturated subunit of strain BE1 fimbriae, reacted with native BE1 fimbriae and appeared to be strain specific. Bacteroides fragilis strain BE38 expressed fimbriae which did not react with the polyclonal or monoclonal antibodies directed against strain BE1 fimbriae.
Department of Plant Quality, Bulb Research Centre, Lisse, The Netherlands.
J
J
van Doorn
B
B
Oudega
D M
DM
MacLaren
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D001441:Bacteroides fragilis / Q000737:chemistry*; D010861:Fimbriae, Bacterial / Q000737:chemistry* / Q000276:immunology; D015151:Immunoblotting; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011233:Precipitin Tests; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
D001426:Bacterial Proteins