title: Molecular characterization of a secreted enzyme with phospholipase B activity from Moraxella bovis.
abstract: A candidate for a vaccine against infectious bovine keratoconjunctivitis (IBK) has been cloned and characterized from Moraxella bovis. The plb gene encodes a protein of 616 amino acids (molecular mass of ~65.8 kDa) that expresses phospholipase B activity. Amino acid sequence analysis revealed that PLB is a new member of the GDSL (Gly-Asp-Ser-Leu) family of lipolytic enzymes.
authors.affiliation: CSIRO Livestock Industries, Geelong, Victoria, Australia 3220. J.Farn@vet.gla.ac.uk
authors.forename: J L
authors.initials: JL
authors.lastname: Farn
authors.forename: R A
authors.initials: RA
authors.lastname: Strugnell
authors.forename: P A
authors.initials: PA
authors.lastname: Hoyne
authors.forename: W P
authors.initials: WP
authors.lastname: Michalski
authors.forename: J M
authors.initials: JM
authors.lastname: Tennent
mesh_terms: D000942:Antigens, Bacterial / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D015153:Blotting, Western; D003001:Cloning, Molecular; D005798:Genes, Bacterial; D008245:Lysophospholipase / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D008969:Molecular Sequence Data; D016955:Moraxella bovis / Q000201:enzymology / Q000235:genetics*; D011994:Recombinant Proteins / Q000378:metabolism; D020539:Sequence Analysis, Protein
chemical_list: D000942:Antigens, Bacterial; D011994:Recombinant Proteins; D008245:Lysophospholipase