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Identification of a 19.3-kDa protein in MRHA-positive Edwardsiella tarda: putative fimbrial major subunit
- Source :
-
FEMS Microbiology Letters . Sep2003, Vol. 226 Issue 1, p127. 7p. - Publication Year :
- 2003
-
Abstract
- The hemagglutinating properties of Edwardsiella tarda isolated from fish were investigated. Hemagglutination of E. tarda was not inhibited by D-mannose but was strongly inhibited by fetuin and N-acetylneuraminic acid. Extraction of hemagglutinating activity from bacterial cells was achieved using n-octyl-β-D-thioglucoside (NOTG), and the NOTG extracts were fractionated by sucrose density gradient ultracentrifugation. Sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis of the fractions revealed that a 19.3-kDa protein band appeared in the fractions exhibiting highest hemagglutinating activity. In an immunoblot analysis of NOTG extracts from 18 strains of E. tarda, the 19.3-kDa protein was detected only in the extracts possessing hemagglutinating activity. The predicted amino acid sequence of a 534-bp gene encoding the 19.3-kDa protein was identical to fimbrial subunit (FimA) of E. tarda by FASTA homology search. These findings suggest that fimbriae are implicated in the hemagglutination of E. tarda. [Copyright &y& Elsevier]
- Subjects :
- *PILI (Microbiology)
*BLOOD agglutination
*ELECTROPHORESIS
Subjects
Details
- Language :
- English
- ISSN :
- 03781097
- Volume :
- 226
- Issue :
- 1
- Database :
- Academic Search Index
- Journal :
- FEMS Microbiology Letters
- Publication Type :
- Academic Journal
- Accession number :
- 10807123
- Full Text :
- https://doi.org/10.1016/S0378-1097(03)00608-6