Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Journal of fish diseases - 1 Nov 2007

Naka H, Hirono I, Aoki T

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Erythrocytes
Share to Fishes
Share to Hemolysis

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mammals

Share to Phospholipases

Share to Recombinant Proteins

Share to Sequence Alignment

Share to Sequence Homology, Amino Acid

Source

Identifiers

PMID: 17958612
DOI: 10.1111/j.1365-2761.2007.00861.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Cloning and characterization of Photobacterium damselae ssp. piscicida phospholipase: an enzyme that shows haemolytic activity.PMID 17958612Read ↗

A virulence gene typing scheme for Photobacterium damselae subsp. piscicida, the causative agent of fish photobacteriosis, reveals a high prevalence of plasmid-encoded virulence factors and of type III secretion system genesSemantic proximity Read ↗

Photobacterium damselae subsp. piscicida: an integrated view of a bacterial fish pathogen.Semantic proximity Read ↗

Evidence for horizontal gene transfer, gene duplication and genetic variation as driving forces of the diversity of haemolytic phenotypes in Photobacterium damselae subsp. damselae.Semantic proximity Read ↗

Genotypic diversity, and molecular and pathogenic characterization of Photobacterium damselae subsp. piscicida isolated from different fish species in Taiwan.Semantic proximity Read ↗

Structure and Biosynthetic Assembly of Piscibactin, a Siderophore from <i>Photobacterium damselae</i> subsp. <i>piscicida</i>, Predicted from Genome AnalysisSemantic proximity Read ↗

Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinaseSemantic proximity Read ↗

Phospholipase PlaB of Legionella pneumophila Represents a Novel Lipase FamilySemantic proximity Read ↗

Genetic diversity of Australian isolates of Photobacterium damselae subsp. damselae is associated with virulence to yellowtail kingfish (Seriola lalandi)Semantic proximity Read ↗

Photobacterium damselae subsp. damselae major virulence factors Dly, plasmid-encoded HlyA, and chromosome-encoded HlyA are secreted via the type II secretion system.Semantic proximity Read ↗

Photobacterium lipolyticum sp. nov., a bacterium with lipolytic activity isolated from the Yellow Sea in Korea.Semantic proximity Read ↗

Phenotypic characterization of the marine pathogen Photobacterium damselae subsp. piscicida.Semantic proximity Read ↗

Cloning and characterization of the gene encoding the major cell-associated phospholipase A of Legionella pneumophila, plaB, exhibiting hemolytic activity.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.