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Molecular characterization of a secreted enzyme with phospholipase B activity from Moraxella bovis.
Farn, J L; Strugnell, R A; Hoyne, P A; Michalski, W P; Tennent, J M.
J Bacteriol ; 183(22): 6717-20, 2001 Nov.
Article in English | MEDLINE | ID: mdl-11673447

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.


Subject(s)
Genes, Bacterial , Lysophospholipase/genetics , Moraxella bovis/genetics , Antigens, Bacterial/genetics , Antigens, Bacterial/isolation & purification , Antigens, Bacterial/metabolism , Blotting, Western , Cloning, Molecular , Lysophospholipase/isolation & purification , Lysophospholipase/metabolism , Molecular Sequence Data , Moraxella bovis/enzymology , Recombinant Proteins/metabolism , Sequence Analysis, Protein
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