ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1016/S0378-1097(03)00608-6
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