Please use this identifier to cite or link to this item:
Title: Cloning, characterisation and expression of Aeromonas hydrophila major adhesin
Authors: Fang, H.-M.
Ge, R. 
Sin, Y.M. 
Keywords: A. hydrophila
Outer membrane protein
Issue Date: May-2004
Citation: Fang, H.-M., Ge, R., Sin, Y.M. (2004-05). Cloning, characterisation and expression of Aeromonas hydrophila major adhesin. Fish and Shellfish Immunology 16 (5) : 645-658. ScholarBank@NUS Repository.
Abstract: Aeromonas hydrophila, an important pathogen in fish, is believed to cause diseases by adhesive and enterotoxic mechanisms. The adhesion is a prerequisite for successful invasion. In this study, the gene of a 43 kDa major adhesin (designated as AHA1) was cloned and expressed. Nucleotide sequence analysis of AHA1 revealed an open reading frame encoding a polypeptide of 373 amino acids with a 20-amino-acid putative signal peptide (molecular weight 40,737 Da). The amino acid sequences of Aha1p showed a very high homology with the other two outer membrane proteins of A. hydrophila. Using the T-5 expression system, this major adhesin Aha1p was expressed in Escherichia coli. The purified recombinant adhesin could competitively inhibit A. hydrophila from invading fish epithelial cells in vitro. Western-blot analysis showed that this major adhesin is a very conserved antigen among various strains of Aeromonas. When used to immunise blue gourami, the recombinant adhesin could confer significant protection to fish against experimental A. hydrophila challenge. © 2004 Elsevier Ltd. All rights reserved.
Source Title: Fish and Shellfish Immunology
ISSN: 10504648
DOI: 10.1016/j.fsi.2003.10.003
Appears in Collections:Staff Publications

Show full item record
Files in This Item:
There are no files associated with this item.

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.