Mycoplasma bovis Membrane Protein MilA Is a Multifunctional Lipase with Novel Lipid and Glycosaminoglycan Binding Activity
James Yazah Adamu, Nadeeka Kumari Wawegama, Anna Kanci Condello, Marc Serge Marenda, Philip Francis Markham, Glenn Francis Browning, Kelly Anne Tivendale
Infection and Immunity | AMER SOC MICROBIOLOGY | Published : 2020
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. We mutagenized the gene to facilitate expression of a series of regions spanning ..View full abstract
James Yazah Adamu was supported by MIFRS and MIRS scholarships from The University of Melbourne and by a Staff Study Fellowship from the University of Maiduguri.