2020
DOI: 10.1128/iai.00945-19
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Mycoplasma bovis Membrane Protein MilA Is a Multifunctional Lipase with Novel Lipid and Glycosaminoglycan Binding Activity

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 … Show more

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Cited by 12 publications
(17 citation statements)
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“…Indeed, purified, recombinant BB0562 demonstrated lipase activity, which was dependent on the serine residues in the two canonical GXSXG lipase motifs identified in the protein. In bacteria, lipases have been predominantly shown to be secreted extracellularly [ 40 , 42 ] and there are some examples of lipases that localize to the bacterial outer surface [ 63 , 64 ], both of which likely allow interaction of the lipase with target substrates in the environment. Our data indicate that BB0562 is associated with the spirochete outer membrane but is likely not surface exposed.…”
Section: Discussionmentioning
confidence: 99%
“…Indeed, purified, recombinant BB0562 demonstrated lipase activity, which was dependent on the serine residues in the two canonical GXSXG lipase motifs identified in the protein. In bacteria, lipases have been predominantly shown to be secreted extracellularly [ 40 , 42 ] and there are some examples of lipases that localize to the bacterial outer surface [ 63 , 64 ], both of which likely allow interaction of the lipase with target substrates in the environment. Our data indicate that BB0562 is associated with the spirochete outer membrane but is likely not surface exposed.…”
Section: Discussionmentioning
confidence: 99%
“…M. hyopneumoniae P65 surface lipoprotein is a lipolytic enzyme with lipase and esterase activities that can hydrolyze short-chain fatty acids on the host cell membrane as its own energy source, but its pathogenic role remains unknown [235]. In addition, M. bovis surface-localized heparin-binding hypothetical adhesin MilA is an immunoreactive, multifunctional enzyme that comprises lipase, ATPase, lipid-binding, and glycosaminoglycan-binding activities, thus contributing to the pathogenesis of M. bovis infection [12]. milA homologues have been found in the genomes of numerous mycoplasmas, including M. agalactiae, M. fermentans, M. hyopneumoniae, M. arginini, and M. gallisepticum.…”
Section: Lipolytic Enzymesmentioning
confidence: 99%
“…milA homologues have been found in the genomes of numerous mycoplasmas, including M. agalactiae, M. fermentans, M. hyopneumoniae, M. arginini, and M. gallisepticum. The presence of the Lipase_GDSL_2 motif is a common characteristic of these milA homologous genes [12]. Similarly, comparative genome sequencing manifested that some lipase homologous genes have also been found in M. pneumoniae and M. genitalium, but their functions in pathogenesis remain to be fully understood.…”
Section: Lipolytic Enzymesmentioning
confidence: 99%
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“…Mycoplasma lack cell walls, and since the cytoplasmic membrane components are directly in contact with host cells, they are generally thought to play an important role in survival, replication, and virulence compared to those in other bacterial species with cell walls ( 22 ); however, many mycoplasma proteins remain hypothetical ( 23 ). Many mycoplasma gene products have little or no detectable sequence similarity to those characterized in other bacteria ( 24 ).…”
Section: Introductionmentioning
confidence: 99%