Cloning and characterization of Photobacterium damselae ssp. piscicida phospholipase : an enzyme that shows haemolytic activity

A phospholipase gene of Photobacterium damselae ssp. piscicida (ppp) was cloned from a genomic library and its nucleotide sequence was determined. The open reading frame consisted of 1218 bp encoding a protein of 405 amino acids with a predicted molecular mass of 46 kDa. The PPP had identities (53-5...

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Veröffentlicht in:Journal of fish diseases. - 1998. - 30(2007), 11 vom: 23. Nov., Seite 681-90
1. Verfasser: Naka, H (VerfasserIn)
Weitere Verfasser: Hirono, I, Aoki, T
Format: Aufsatz
Sprache:English
Veröffentlicht: 2007
Zugriff auf das übergeordnete Werk:Journal of fish diseases
Schlagworte:Journal Article DNA, Bacterial Recombinant Proteins Phospholipases EC 3.1.-
Beschreibung
Zusammenfassung:A phospholipase gene of Photobacterium damselae ssp. piscicida (ppp) was cloned from a genomic library and its nucleotide sequence was determined. The open reading frame consisted of 1218 bp encoding a protein of 405 amino acids with a predicted molecular mass of 46 kDa. The PPP had identities (53-55%) with phospholipase and haemolysin of Vibrio spp., while it showed low identities (23-26%) with glycerophospholipid cholesterol acyltransferase of Aeromonas spp. A recombinant PPP (rPPP) with a His tag at the C-terminus expressed in Escherichia coli and purified showed phospholipase activity. The rPPP also showed lecithin-dependent haemolytic activity against mammalian erythrocytes and direct haemolytic activity against fish erythrocytes. The culture supernatant of wild-type P. damselae ssp. piscicida showed phospholipase activity, while that of a PPP gene knockout mutant did not
Beschreibung:Date Completed 05.02.2008
Date Revised 30.09.2020
published: Print
GENBANK: AB071137
Citation Status MEDLINE
ISSN:0140-7775