Mycoplasma bovis Membrane Protein MilA Is a Multifunctional Lipase with Novel Lipid and Glycosaminoglycan Binding Activity
J. Adamu, Nadeeka K. Wawegama, Anna Kanci, Marc S. Marenda, Philip F. Markham, Glenn F. Browning, Kelly A. Tivendale
Abstract
The survival, replication, and virulence of mycoplasmas depend on their ability to capture and import host-derived nutrients using poorly characterized membrane proteins. Previous studies on the important bovine pathogen Mycoplasma bovis demonstrated that the amino-terminal end of an immunogenic 226-kDa (P226) protein, encoded by milA (the full-length product of which has a predicted molecular weight of 303 kDa), had lipase activity. The predicted sequence of MilA contains glycosaminoglycan binding motifs, as well as multiple copies of a domain of unknown function (DUF445) that is also found in apolipoproteins.
Topics & Concepts
BiologyLipasePathogenBiochemistryMicrobiologyGlycoproteinPeptide sequenceBacteriaHepatic lipaseEnzymeGeneGeneticsMicrobial infections and disease researchToxoplasma gondii Research StudiesBlood groups and transfusion