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|Title:||Cloning, characterisation and expression of Aeromonas hydrophila major adhesin||Authors:||Fang, H.-M.
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. https://doi.org/10.1016/j.fsi.2003.10.003||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||URI:||http://scholarbank.nus.edu.sg/handle/10635/100285||ISSN:||10504648||DOI:||10.1016/j.fsi.2003.10.003|
|Appears in Collections:||Staff Publications|
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