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- W2743130081 abstract "Abstract Protein O -mannosylation is crucial for the biology of Mycobacterium tuberculosis but the key mannosylated protein(s) involved and its(their) underlying function(s) remain unknown. Here, we demonstrated that the M . tuberculosis mutant (Δ pmt ) deficient for protein O -mannosylation exhibits enhanced release of lipoarabinomannan (LAM) in a complex with LprG, a lipoprotein required for LAM translocation to the cell surface. We determined that LprG is O- mannosylated at a unique threonine position by mass spectrometry analyses of the purified protein. However, although replacement of this amino acid by an alanine residue completely abolished LprG O- mannosylation, the increased release of the LAM/LprG complex was preserved. We found that the increased secretion of this complex is due to enhanced LAM production in the Δ pmt M . tuberculosis and M . smegmatis mutants relative to their wild-type counterparts. This abnormal release of LAM/LprG has functional consequences on the induction of inflammatory responses and provides a possible explanation for the reduced virulence of the M . tuberculosis Δ pmt mutant." @default.
- W2743130081 created "2017-08-17" @default.
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- W2743130081 date "2017-08-11" @default.
- W2743130081 modified "2023-10-16" @default.
- W2743130081 title "Protein O-mannosylation deficiency increases LprG-associated lipoarabinomannan release by Mycobacterium tuberculosis and enhances the TLR2-associated inflammatory response" @default.
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- W2743130081 doi "https://doi.org/10.1038/s41598-017-08489-7" @default.
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