Acinetobacter baumannii outer membrane protein A induces HeLa cell autophagy via MAPK/JNK signaling pathway.
Identifieur interne : 000394 ( Main/Exploration ); précédent : 000393; suivant : 000395Acinetobacter baumannii outer membrane protein A induces HeLa cell autophagy via MAPK/JNK signaling pathway.
Auteurs : Zhiyuan An [République populaire de Chine] ; Xiaoxi Huang [République populaire de Chine] ; Chunming Zheng [République populaire de Chine] ; Wenyi Ding [République populaire de Chine]Source :
- International journal of medical microbiology : IJMM [ 1618-0607 ] ; 2019.
Descripteurs français
- KwdFr :
- Acinetobacter baumannii (immunologie), Animaux (MeSH), Autophagie (MeSH), Cellules HeLa (immunologie), Cellules HeLa (microbiologie), Cellules RAW 264.7 (MeSH), Humains (MeSH), Protéines de la membrane externe bactérienne (métabolisme), Sirolimus (métabolisme), Souris (MeSH), Survie cellulaire (effets des médicaments et des substances chimiques), Système de signalisation des MAP kinases (MeSH).
- MESH :
- effets des médicaments et des substances chimiques : Survie cellulaire.
- immunologie : Acinetobacter baumannii, Cellules HeLa.
- microbiologie : Cellules HeLa.
- métabolisme : Protéines de la membrane externe bactérienne, Sirolimus.
- Animaux, Autophagie, Cellules RAW 264.7, Humains, Souris, Système de signalisation des MAP kinases.
English descriptors
- KwdEn :
- Acinetobacter baumannii (immunology), Animals (MeSH), Autophagy (MeSH), Bacterial Outer Membrane Proteins (metabolism), Cell Survival (drug effects), HeLa Cells (immunology), HeLa Cells (microbiology), Humans (MeSH), MAP Kinase Signaling System (MeSH), Mice (MeSH), RAW 264.7 Cells (MeSH), Sirolimus (metabolism).
- MESH :
- chemical , metabolism : Bacterial Outer Membrane Proteins, Sirolimus.
- drug effects : Cell Survival.
- immunology : Acinetobacter baumannii, HeLa Cells.
- microbiology : HeLa Cells.
- Animals, Autophagy, Humans, MAP Kinase Signaling System, Mice, RAW 264.7 Cells.
Abstract
Autophagy is an evolutionary conserved self-balancing process that plays an important role in maintaining cellular homeostasis via the clearance of damaged organelles and misfolded proteins. Infection-triggered autophagy specifically inhibits the invasion of intracellular bacterial replication and hence protects the cells from microbial infections. It has been reported that Acinetobacter baumannii trigger cell autophagy. However, the role of its virulence protein OmpA remains unclear. Therefore, this study aimed to explore the effects of Acinetobacter baumannii OmpA on cell autophagy and its underlying molecular mechanisms. The results showed that OmpA induced autophagy in HeLa and RAW264.7 cells, increased LC3BII expression, and hindered p62 degradation. Moreover, OmpA triggered incomplete autophagy by interfering the fusion of autophagosomes with lysosomes. Besides, OmpA activated MAPK/JNK signaling pathway and enhanced the phosphorylation levels of JNK, p38, and ERK, c-Jun. Inhibition of JNK signaling pathway suppressed OmpA-induced autophagy in HeLa cells. Ab wild-type strains carrying OmpA triggered incomplete autophagy and resulted in a large number of IL-1β production. Ab-△OmpA strain (OmpA gene mutation) restored autophagic flux and reduced the accumulation of p62 and the release of IL-1β in HeLa cells. Rapamycin activated autophagy to inhibit OmpA-induced IL-1β secretion and protect HeLa cells from inflammatory damage. Collectively, these results suggest that OmpA can induce autophagy in HeLa cells through MAPK/JNK signaling pathway. Pre-treatment with Rapamycin activates autophagy and protects against cell death.
DOI: 10.1016/j.ijmm.2018.12.004
PubMed: 30606692
Affiliations:
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xml:lang="en">Autophagy is an evolutionary conserved self-balancing process that plays an important role in maintaining cellular homeostasis via the clearance of damaged organelles and misfolded proteins. Infection-triggered autophagy specifically inhibits the invasion of intracellular bacterial replication and hence protects the cells from microbial infections. It has been reported that Acinetobacter baumannii trigger cell autophagy. However, the role of its virulence protein OmpA remains unclear. Therefore, this study aimed to explore the effects of Acinetobacter baumannii OmpA on cell autophagy and its underlying molecular mechanisms. The results showed that OmpA induced autophagy in HeLa and RAW264.7 cells, increased LC3BII expression, and hindered p62 degradation. Moreover, OmpA triggered incomplete autophagy by interfering the fusion of autophagosomes with lysosomes. Besides, OmpA activated MAPK/JNK signaling pathway and enhanced the phosphorylation levels of JNK, p38, and ERK, c-Jun. Inhibition of JNK signaling pathway suppressed OmpA-induced autophagy in HeLa cells. Ab wild-type strains carrying OmpA triggered incomplete autophagy and resulted in a large number of IL-1β production. Ab-△OmpA strain (OmpA gene mutation) restored autophagic flux and reduced the accumulation of p62 and the release of IL-1β in HeLa cells. Rapamycin activated autophagy to inhibit OmpA-induced IL-1β secretion and protect HeLa cells from inflammatory damage. Collectively, these results suggest that OmpA can induce autophagy in HeLa cells through MAPK/JNK signaling pathway. Pre-treatment with Rapamycin activates autophagy and protects against cell death.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">30606692</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>10</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1618-0607</ISSN><JournalIssue CitedMedium="Internet"><Volume>309</Volume><Issue>2</Issue><PubDate><Year>2019</Year><Month>Mar</Month></PubDate></JournalIssue><Title>International journal of medical microbiology : IJMM</Title><ISOAbbreviation>Int J Med Microbiol</ISOAbbreviation></Journal><ArticleTitle>Acinetobacter baumannii outer membrane protein A induces HeLa cell autophagy via MAPK/JNK signaling pathway.</ArticleTitle><Pagination><MedlinePgn>97-107</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1438-4221(18)30266-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.ijmm.2018.12.004</ELocationID><Abstract><AbstractText>Autophagy is an evolutionary conserved self-balancing process that plays an important role in maintaining cellular homeostasis via the clearance of damaged organelles and misfolded proteins. Infection-triggered autophagy specifically inhibits the invasion of intracellular bacterial replication and hence protects the cells from microbial infections. It has been reported that Acinetobacter baumannii trigger cell autophagy. However, the role of its virulence protein OmpA remains unclear. Therefore, this study aimed to explore the effects of Acinetobacter baumannii OmpA on cell autophagy and its underlying molecular mechanisms. The results showed that OmpA induced autophagy in HeLa and RAW264.7 cells, increased LC3BII expression, and hindered p62 degradation. Moreover, OmpA triggered incomplete autophagy by interfering the fusion of autophagosomes with lysosomes. Besides, OmpA activated MAPK/JNK signaling pathway and enhanced the phosphorylation levels of JNK, p38, and ERK, c-Jun. Inhibition of JNK signaling pathway suppressed OmpA-induced autophagy in HeLa cells. Ab wild-type strains carrying OmpA triggered incomplete autophagy and resulted in a large number of IL-1β production. Ab-△OmpA strain (OmpA gene mutation) restored autophagic flux and reduced the accumulation of p62 and the release of IL-1β in HeLa cells. Rapamycin activated autophagy to inhibit OmpA-induced IL-1β secretion and protect HeLa cells from inflammatory damage. Collectively, these results suggest that OmpA can induce autophagy in HeLa cells through MAPK/JNK signaling pathway. Pre-treatment with Rapamycin activates autophagy and protects against cell death.</AbstractText><CopyrightInformation>Copyright © 2019 Elsevier GmbH. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>An</LastName><ForeName>Zhiyuan</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Medical Research Center, Beijing Chaoyang Hospital, Capital Medical University, Beijing 100020, China. 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MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001343" MajorTopicYN="Y">Autophagy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001425" MajorTopicYN="N">Bacterial Outer Membrane Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002470" MajorTopicYN="N">Cell Survival</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006367" MajorTopicYN="N">HeLa Cells</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName 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