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iNature is believed that mitochondria originated about 2.
5 billion years ago.
Mitochondria not only produce energy in the cell, but they also play a role in defending against bacterial pathogens.
Although the morphology and function of mitochondria have undergone tremendous changes after bacterial attack, it is still unknown whether the bacteria in the cell can hijack mitochondria to promote their survival.
On January 18, 2021, the Ohio State University Wen Haitao and Shandong University Wang Haibo jointly published a research paper entitled "Listeria monocytogenes upregulates mitochondrial calcium signalling to inhibit LC3-associated phagocytosis as a survival strategy" in Nature Microbiology.
The research found Listeria monocytogenes (an intracellular bacterial pathogen) inhibits LC3-related phagocytosis (LAP) by regulating mitochondrial Ca2 + (mtCa2 +) signaling in order to survive in the cell.
Listeria monocytogenes invaded macrophages through mtCa2 + uniporter (MCU) to induce mtCa2 + uptake, thereby increasing the production of acetyl-CoA produced by pyruvate dehydrogenase.
The acetylation of LAP effector Rubicon and acetyl-CoA can reduce the formation of LAP.
Due to the increased formation of LAP, the genetic deletion of the MCU reduces the growth of bacteria in the cell.
The research data shows that regulating mtCa2 + signal transduction can improve the survival rate of bacteria in the cell, and emphasizes the importance of mitochondrial metabolism in the interaction between the host and the microorganism.
The co-evolution between mitochondria and host cells began 2.
5 billion years ago, when ancient α-proteobacteria were swallowed by endophytic bacteria through archaea.
Mitochondria have at least two main functions: energy production and innate immunity against invading pathogens.
Mitochondria are metabolically active organelles that can convert organic molecules into energy in the presence of oxygen and produce intermediate metabolites for the synthesis of macromolecules.
Mitochondria can also coordinate many immune functions.
The release of risk-related molecular patterns derived from mitochondria can induce the activation of innate immune cells.
Mitochondria provide a membrane platform for the assembly of multiple innate immune complexes.
The contact site between the mitochondria and the endoplasmic reticulum provides an isolation membrane for the formation of autophagosomes.
In addition, several mitochondrial metabolic enzymes, including succinate dehydrogenase and immune response gene 1, as well as intermediate mitochondrial metabolites, have been reported to be involved in immune activation or bacterial killing.
Recent studies have shown that after bacterial invasion, close crosstalk occurs between mitochondria and phagosomes.
For example, after bacterial infection, Toll-like receptor (TLR) signals from the phagosome are transferred to the mitochondria to recruit to the phagosome and promote bacterial killing.
Mitochondria can also release vesicles containing reactive oxygen species (ROS) into phagosomes containing bacteria to kill bacteria.
However, it has not been studied whether intracellular bacteria can manipulate mitochondrial-phagosome interactions.
Mitochondrial Ca2 + (mtCa2 +) signaling is the basic mechanism for regulating mitochondrial metabolism by targeting key enzymes involved in the tricarboxylic acid (TCA) cycle.
Pyruvate dehydrogenase (PDH) is a key enzyme for the production of mitochondrial acetyl-CoA.
It requires Ca2+ to maintain its enzymatic activity.
The mtCa2 + uniporter (MCU) is a highly selective Ca2 + channel.
Due to the strong mobilization of mtCa2+ during bacterial attack, this is particularly relevant for host-bacterial interactions.
MCU-dependent mitochondrial metabolism may play an important role in the antibacterial response.
LC3-related phagocytosis (LAP) has recently been described as an essential defense mechanism against invading pathogens.
LAP is different from typical autophagy.
It uses a unique initiation complex composed of UVRAG (ultraviolet radiation-related genes) Beclin-1 and VPS34 (vacuum protein sorting 34) and a unique regulator Rubicon, etc.
.
Although the molecular composition of LAP is clear, the mechanism that regulates LAP assembly and activity is not yet fully understood.
The study found that the infection of Listeria monocytogenes promotes the MCU-mediated production of acetyl-CoA, which is essential for Rubicon acetylation, which negatively regulates the assembly of LAP and the killing of bacteria.
The absence of MCU in myeloid cells greatly increases LAP activity, thereby improving the cell's anti-Listeria response.
The study believes that Listeria's regulation of MCU-acetyl-CoA metabolism is a survival strategy, which may be shared by other intracellular pathogens.
Reference message: https://
5 billion years ago.
Mitochondria not only produce energy in the cell, but they also play a role in defending against bacterial pathogens.
Although the morphology and function of mitochondria have undergone tremendous changes after bacterial attack, it is still unknown whether the bacteria in the cell can hijack mitochondria to promote their survival.
On January 18, 2021, the Ohio State University Wen Haitao and Shandong University Wang Haibo jointly published a research paper entitled "Listeria monocytogenes upregulates mitochondrial calcium signalling to inhibit LC3-associated phagocytosis as a survival strategy" in Nature Microbiology.
The research found Listeria monocytogenes (an intracellular bacterial pathogen) inhibits LC3-related phagocytosis (LAP) by regulating mitochondrial Ca2 + (mtCa2 +) signaling in order to survive in the cell.
Listeria monocytogenes invaded macrophages through mtCa2 + uniporter (MCU) to induce mtCa2 + uptake, thereby increasing the production of acetyl-CoA produced by pyruvate dehydrogenase.
The acetylation of LAP effector Rubicon and acetyl-CoA can reduce the formation of LAP.
Due to the increased formation of LAP, the genetic deletion of the MCU reduces the growth of bacteria in the cell.
The research data shows that regulating mtCa2 + signal transduction can improve the survival rate of bacteria in the cell, and emphasizes the importance of mitochondrial metabolism in the interaction between the host and the microorganism.
The co-evolution between mitochondria and host cells began 2.
5 billion years ago, when ancient α-proteobacteria were swallowed by endophytic bacteria through archaea.
Mitochondria have at least two main functions: energy production and innate immunity against invading pathogens.
Mitochondria are metabolically active organelles that can convert organic molecules into energy in the presence of oxygen and produce intermediate metabolites for the synthesis of macromolecules.
Mitochondria can also coordinate many immune functions.
The release of risk-related molecular patterns derived from mitochondria can induce the activation of innate immune cells.
Mitochondria provide a membrane platform for the assembly of multiple innate immune complexes.
The contact site between the mitochondria and the endoplasmic reticulum provides an isolation membrane for the formation of autophagosomes.
In addition, several mitochondrial metabolic enzymes, including succinate dehydrogenase and immune response gene 1, as well as intermediate mitochondrial metabolites, have been reported to be involved in immune activation or bacterial killing.
Recent studies have shown that after bacterial invasion, close crosstalk occurs between mitochondria and phagosomes.
For example, after bacterial infection, Toll-like receptor (TLR) signals from the phagosome are transferred to the mitochondria to recruit to the phagosome and promote bacterial killing.
Mitochondria can also release vesicles containing reactive oxygen species (ROS) into phagosomes containing bacteria to kill bacteria.
However, it has not been studied whether intracellular bacteria can manipulate mitochondrial-phagosome interactions.
Mitochondrial Ca2 + (mtCa2 +) signaling is the basic mechanism for regulating mitochondrial metabolism by targeting key enzymes involved in the tricarboxylic acid (TCA) cycle.
Pyruvate dehydrogenase (PDH) is a key enzyme for the production of mitochondrial acetyl-CoA.
It requires Ca2+ to maintain its enzymatic activity.
The mtCa2 + uniporter (MCU) is a highly selective Ca2 + channel.
Due to the strong mobilization of mtCa2+ during bacterial attack, this is particularly relevant for host-bacterial interactions.
MCU-dependent mitochondrial metabolism may play an important role in the antibacterial response.
LC3-related phagocytosis (LAP) has recently been described as an essential defense mechanism against invading pathogens.
LAP is different from typical autophagy.
It uses a unique initiation complex composed of UVRAG (ultraviolet radiation-related genes) Beclin-1 and VPS34 (vacuum protein sorting 34) and a unique regulator Rubicon, etc.
.
Although the molecular composition of LAP is clear, the mechanism that regulates LAP assembly and activity is not yet fully understood.
The study found that the infection of Listeria monocytogenes promotes the MCU-mediated production of acetyl-CoA, which is essential for Rubicon acetylation, which negatively regulates the assembly of LAP and the killing of bacteria.
The absence of MCU in myeloid cells greatly increases LAP activity, thereby improving the cell's anti-Listeria response.
The study believes that Listeria's regulation of MCU-acetyl-CoA metabolism is a survival strategy, which may be shared by other intracellular pathogens.
Reference message: https://
