biostudies-literatureUnknown13Margenat MDuring <i>Mycobacterium tuberculosis (Mtb)</i> infection, the virulence factor PtpA belonging to the protein tyrosine phosphatase family is delivered into the cytosol of the macrophage. PtpA interacts with numerous eukaryotic proteins modulating phagosome maturation, innate immune response, apoptosis, and potentially host-lipid metabolism, as previously reported by our group. <i>In vitro</i>, the human trifunctional protein enzyme (<i>h</i>TFP) is a <i>bona fide</i> PtpA substrate, a key enzyme of mitochondrial β-oxidation of long-chain fatty acids, containing two alpha and two beta subunits arranged in a tetramer structure. Interestingly, it has been described that the alpha subunit of <i>h</i>TFP (ECHA, <i>h</i>TFPα) is no longer detected in mitochondria during macrophage infection with Frontiers in cellular and infection microbiology1095060https://www.ebi.ac.uk/biostudies/studies/S-EPMC10325834biostudies-literatureCharacteristics of <i>Mycobacterium tuberculosis</i> PtpA interaction and activity on the alpha subunit of human mitochondrial trifunctional protein, a key enzyme of lipid metabolism.PMC10325834Margenat MCarrion FVillarino APortela MMIrving VHerrera FEBetancour GGarcia-Cedres TCostabile AfalseCharacteristics of <i>Mycobacterium tuberculosis</i> PtpA interaction and activity on the alpha subunit of human mitochondrial trifunctional protein, a key enzyme of lipid metabolism.During <i>Mycobacterium tuberculosis (Mtb)</i> infection, the virulence factor PtpA belonging to the protein tyrosine phosphatase family is delivered into the cytosol of the macrophage. PtpA interacts with numerous eukaryotic proteins modulating phagosome maturation, innate immune response, apoptosis, and potentially host-lipid metabolism, as previously reported by our group. <i>In vitro</i>, the human trifunctional protein enzyme (<i>h</i>TFP) is a <i>bona fide</i> PtpA substrate, a key enzyme of mitochondrial β-oxidation of long-chain fatty acids, containing two alpha and two beta subunits arranged in a tetramer structure. Interestingly, it has been described that the alpha subunit of <i>h</i>TFP (ECHA, <i>h</i>TFPα) is no longer detected in mitochondria during macrophage infection with 2023-01-01T00:00:00Z20232026-05-29T00:28:45.182Z2025-02-19T04:25:56.358ZS-EPMC103258343742479010.3389/fcimb.2023.1095060