Journal Article

Identification of a 19.3-kDa protein in MRHA-positive <i>Edwardsiella tarda</i>: putative fimbrial major subunit

Takamitsu Sakai, Kinya Kanai, Kiyoshi Osatomi and Kazuma Yoshikoshi

in FEMS Microbiology Letters

Volume 226, issue 1, pages 127-133
Published in print September 2003 |
Published online January 2006 | e-ISSN: 1574-6968 | DOI:

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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.

Keywords: Edwardsiella tarda; Hemagglutination; Fimbria

Journal Article.  3288 words.  Illustrated.

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