Molecular characterization of a secreted enzyme with phospholipase B activity from Moraxella bovis.
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.
Farn
J L
JL
CSIRO Livestock Industries, Geelong, Victoria, Australia 3220. J.Farn@vet.gla.ac.uk
Strugnell
R A
RA
Hoyne
P A
PA
Michalski
W P
WP
Tennent
J M
JM
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
D000942:Antigens, Bacterial; D011994:Recombinant Proteins; D008245:Lysophospholipase