Inhibition of autophagy ameliorates acute lung injury caused by avian influenza A H5N1 infection.
Identifieur interne : 001185 ( Main/Corpus ); précédent : 001184; suivant : 001186Inhibition of autophagy ameliorates acute lung injury caused by avian influenza A H5N1 infection.
Auteurs : Yang Sun ; Chenggang Li ; Yuelong Shu ; Xiangwu Ju ; Zhen Zou ; Hongliang Wang ; Shuan Rao ; Feng Guo ; Haolin Liu ; Wenlong Nan ; Yan Zhao ; Yiwu Yan ; Jun Tang ; Chen Zhao ; Peng Yang ; Kangtai Liu ; Shunxin Wang ; Huijun Lu ; Xiao Li ; Lei Tan ; Rongbao Gao ; Jingdong Song ; Xiang Gao ; Xinlun Tian ; Yingzhi Qin ; Kai-Feng Xu ; Dangsheng Li ; Ningyi Jin ; Chengyu JiangSource :
- Science signaling [ 1937-9145 ] ; 2012.
English descriptors
- KwdEn :
- Analysis of Variance (MeSH), Animals (MeSH), Autophagy (drug effects), Autophagy (physiology), Autophagy-Related Protein 5 (MeSH), Blotting, Western (MeSH), Cell Line (MeSH), DNA Primers (genetics), Epithelial Cells (physiology), Gene Knockdown Techniques (MeSH), Hemagglutinin Glycoproteins, Influenza Virus (administration & dosage), Hemagglutinin Glycoproteins, Influenza Virus (pharmacology), Humans (MeSH), Influenza A Virus, H5N1 Subtype (MeSH), Influenza, Human (pathology), Lung (ultrastructure), Lung (virology), Mice (MeSH), Mice, Inbred BALB C (MeSH), Microscopy, Electron (MeSH), Microtubule-Associated Proteins (genetics), Oncogene Protein v-akt (metabolism), Phagosomes (pathology), Real-Time Polymerase Chain Reaction (MeSH), Signal Transduction (physiology), TOR Serine-Threonine Kinases (metabolism), Tuberous Sclerosis Complex 2 Protein (MeSH), Tumor Suppressor Proteins (metabolism).
- MESH :
- chemical , administration & dosage : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical , genetics : DNA Primers, Microtubule-Associated Proteins.
- chemical , metabolism : Oncogene Protein v-akt, TOR Serine-Threonine Kinases, Tumor Suppressor Proteins.
- chemical , pharmacology : Hemagglutinin Glycoproteins, Influenza Virus.
- chemical : Autophagy-Related Protein 5, Tuberous Sclerosis Complex 2 Protein.
- drug effects : Autophagy.
- pathology : Influenza, Human, Phagosomes.
- physiology : Autophagy, Epithelial Cells, Signal Transduction.
- ultrastructure : Lung.
- virology : Lung.
- Analysis of Variance, Animals, Blotting, Western, Cell Line, Gene Knockdown Techniques, Humans, Influenza A Virus, H5N1 Subtype, Mice, Mice, Inbred BALB C, Microscopy, Electron, Real-Time Polymerase Chain Reaction.
Abstract
The threat of a new influenza pandemic has existed since 1997, when the highly pathogenic H5N1 strain of avian influenza A virus infected humans in Hong Kong and spread across Asia, where it continued to infect poultry and people. The human mortality rate of H5N1 infection is about 60%, whereas that of seasonal H1N1 infection is less than 0.1%. The high mortality rate associated with H5N1 infection is predominantly a result of respiratory failure caused by acute lung injury; however, how viral infection contributes to this disease pathology is unclear. Here, we used electron microscopy to show the accumulation of autophagosomes in H5N1-infected lungs from a human cadaver and mice, as well as in infected A549 human epithelial lung cells. We also showed that H5N1, but not seasonal H1N1, induced autophagic cell death in alveolar epithelial cells through a pathway involving the kinase Akt, the tumor suppressor protein TSC2, and the mammalian target of rapamycin. Additionally, we suggest that the hemagglutinin protein of H5N1 may be responsible for stimulating autophagy. When applied prophylactically, reagents that blocked virus-induced autophagic signaling substantially increased the survival rate of mice and substantially ameliorated the acute lung injury and mortality caused by H5N1 infection. We conclude that the autophagic cell death of alveolar epithelial cells likely plays a crucial role in the high mortality rate of H5N1 infection, and we suggest that autophagy-blocking agents might be useful as prophylactics and therapeutics against infection of humans by the H5N1 virus.
DOI: 10.1126/scisignal.2001931
PubMed: 22355189
Links to Exploration step
pubmed:22355189Le document en format XML
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<affiliation><nlm:affiliation>State Key Laboratory of Medical Molecular Biology, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences, Peking Union Medical College, Tsinghua University, Beijing 100005, P. R. China.</nlm:affiliation>
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<author><name sortKey="Nan, Wenlong" sort="Nan, Wenlong" uniqKey="Nan W" first="Wenlong" last="Nan">Wenlong Nan</name>
</author>
<author><name sortKey="Zhao, Yan" sort="Zhao, Yan" uniqKey="Zhao Y" first="Yan" last="Zhao">Yan Zhao</name>
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<author><name sortKey="Yan, Yiwu" sort="Yan, Yiwu" uniqKey="Yan Y" first="Yiwu" last="Yan">Yiwu Yan</name>
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<author><name sortKey="Zhao, Chen" sort="Zhao, Chen" uniqKey="Zhao C" first="Chen" last="Zhao">Chen Zhao</name>
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<author><name sortKey="Yang, Peng" sort="Yang, Peng" uniqKey="Yang P" first="Peng" last="Yang">Peng Yang</name>
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<author><name sortKey="Wang, Shunxin" sort="Wang, Shunxin" uniqKey="Wang S" first="Shunxin" last="Wang">Shunxin Wang</name>
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<author><name sortKey="Lu, Huijun" sort="Lu, Huijun" uniqKey="Lu H" first="Huijun" last="Lu">Huijun Lu</name>
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<author><name sortKey="Tian, Xinlun" sort="Tian, Xinlun" uniqKey="Tian X" first="Xinlun" last="Tian">Xinlun Tian</name>
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<author><name sortKey="Qin, Yingzhi" sort="Qin, Yingzhi" uniqKey="Qin Y" first="Yingzhi" last="Qin">Yingzhi Qin</name>
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<author><name sortKey="Li, Dangsheng" sort="Li, Dangsheng" uniqKey="Li D" first="Dangsheng" last="Li">Dangsheng Li</name>
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<series><title level="j">Science signaling</title>
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<term>Animals (MeSH)</term>
<term>Autophagy (drug effects)</term>
<term>Autophagy (physiology)</term>
<term>Autophagy-Related Protein 5 (MeSH)</term>
<term>Blotting, Western (MeSH)</term>
<term>Cell Line (MeSH)</term>
<term>DNA Primers (genetics)</term>
<term>Epithelial Cells (physiology)</term>
<term>Gene Knockdown Techniques (MeSH)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (administration & dosage)</term>
<term>Hemagglutinin Glycoproteins, Influenza Virus (pharmacology)</term>
<term>Humans (MeSH)</term>
<term>Influenza A Virus, H5N1 Subtype (MeSH)</term>
<term>Influenza, Human (pathology)</term>
<term>Lung (ultrastructure)</term>
<term>Lung (virology)</term>
<term>Mice (MeSH)</term>
<term>Mice, Inbred BALB C (MeSH)</term>
<term>Microscopy, Electron (MeSH)</term>
<term>Microtubule-Associated Proteins (genetics)</term>
<term>Oncogene Protein v-akt (metabolism)</term>
<term>Phagosomes (pathology)</term>
<term>Real-Time Polymerase Chain Reaction (MeSH)</term>
<term>Signal Transduction (physiology)</term>
<term>TOR Serine-Threonine Kinases (metabolism)</term>
<term>Tuberous Sclerosis Complex 2 Protein (MeSH)</term>
<term>Tumor Suppressor Proteins (metabolism)</term>
</keywords>
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</keywords>
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<term>Microtubule-Associated Proteins</term>
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<term>Tumor Suppressor Proteins</term>
</keywords>
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</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Autophagy-Related Protein 5</term>
<term>Tuberous Sclerosis Complex 2 Protein</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Autophagy</term>
</keywords>
<keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Influenza, Human</term>
<term>Phagosomes</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Autophagy</term>
<term>Epithelial Cells</term>
<term>Signal Transduction</term>
</keywords>
<keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Lung</term>
</keywords>
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<term>Animals</term>
<term>Blotting, Western</term>
<term>Cell Line</term>
<term>Gene Knockdown Techniques</term>
<term>Humans</term>
<term>Influenza A Virus, H5N1 Subtype</term>
<term>Mice</term>
<term>Mice, Inbred BALB C</term>
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<term>Real-Time Polymerase Chain Reaction</term>
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<front><div type="abstract" xml:lang="en">The threat of a new influenza pandemic has existed since 1997, when the highly pathogenic H5N1 strain of avian influenza A virus infected humans in Hong Kong and spread across Asia, where it continued to infect poultry and people. The human mortality rate of H5N1 infection is about 60%, whereas that of seasonal H1N1 infection is less than 0.1%. The high mortality rate associated with H5N1 infection is predominantly a result of respiratory failure caused by acute lung injury; however, how viral infection contributes to this disease pathology is unclear. Here, we used electron microscopy to show the accumulation of autophagosomes in H5N1-infected lungs from a human cadaver and mice, as well as in infected A549 human epithelial lung cells. We also showed that H5N1, but not seasonal H1N1, induced autophagic cell death in alveolar epithelial cells through a pathway involving the kinase Akt, the tumor suppressor protein TSC2, and the mammalian target of rapamycin. Additionally, we suggest that the hemagglutinin protein of H5N1 may be responsible for stimulating autophagy. When applied prophylactically, reagents that blocked virus-induced autophagic signaling substantially increased the survival rate of mice and substantially ameliorated the acute lung injury and mortality caused by H5N1 infection. We conclude that the autophagic cell death of alveolar epithelial cells likely plays a crucial role in the high mortality rate of H5N1 infection, and we suggest that autophagy-blocking agents might be useful as prophylactics and therapeutics against infection of humans by the H5N1 virus.</div>
</front>
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<DateCompleted><Year>2012</Year>
<Month>06</Month>
<Day>15</Day>
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<DateRevised><Year>2018</Year>
<Month>12</Month>
<Day>01</Day>
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<Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1937-9145</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>5</Volume>
<Issue>212</Issue>
<PubDate><Year>2012</Year>
<Month>Feb</Month>
<Day>21</Day>
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<Title>Science signaling</Title>
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<ArticleTitle>Inhibition of autophagy ameliorates acute lung injury caused by avian influenza A H5N1 infection.</ArticleTitle>
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<Abstract><AbstractText>The threat of a new influenza pandemic has existed since 1997, when the highly pathogenic H5N1 strain of avian influenza A virus infected humans in Hong Kong and spread across Asia, where it continued to infect poultry and people. The human mortality rate of H5N1 infection is about 60%, whereas that of seasonal H1N1 infection is less than 0.1%. The high mortality rate associated with H5N1 infection is predominantly a result of respiratory failure caused by acute lung injury; however, how viral infection contributes to this disease pathology is unclear. Here, we used electron microscopy to show the accumulation of autophagosomes in H5N1-infected lungs from a human cadaver and mice, as well as in infected A549 human epithelial lung cells. We also showed that H5N1, but not seasonal H1N1, induced autophagic cell death in alveolar epithelial cells through a pathway involving the kinase Akt, the tumor suppressor protein TSC2, and the mammalian target of rapamycin. Additionally, we suggest that the hemagglutinin protein of H5N1 may be responsible for stimulating autophagy. When applied prophylactically, reagents that blocked virus-induced autophagic signaling substantially increased the survival rate of mice and substantially ameliorated the acute lung injury and mortality caused by H5N1 infection. We conclude that the autophagic cell death of alveolar epithelial cells likely plays a crucial role in the high mortality rate of H5N1 infection, and we suggest that autophagy-blocking agents might be useful as prophylactics and therapeutics against infection of humans by the H5N1 virus.</AbstractText>
</Abstract>
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<ForeName>Yuelong</ForeName>
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<ForeName>Xiangwu</ForeName>
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<ForeName>Chen</ForeName>
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<Author ValidYN="Y"><LastName>Liu</LastName>
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<ForeName>Huijun</ForeName>
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<ForeName>Xiao</ForeName>
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<ForeName>Lei</ForeName>
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<ForeName>Rongbao</ForeName>
<Initials>R</Initials>
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<Author ValidYN="Y"><LastName>Song</LastName>
<ForeName>Jingdong</ForeName>
<Initials>J</Initials>
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<ForeName>Xiang</ForeName>
<Initials>X</Initials>
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<Initials>X</Initials>
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<Initials>Y</Initials>
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<Initials>D</Initials>
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<ForeName>Chengyu</ForeName>
<Initials>C</Initials>
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<Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>0</RegistryNumber>
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<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C000624654">Tsc2 protein, mouse</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
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<QualifierName UI="Q000473" MajorTopicYN="Y">pathology</QualifierName>
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<MeshHeading><DescriptorName UI="D008168" MajorTopicYN="N">Lung</DescriptorName>
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<MeshHeading><DescriptorName UI="D051379" MajorTopicYN="N">Mice</DescriptorName>
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<MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName>
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<MeshHeading><DescriptorName UI="D008869" MajorTopicYN="N">Microtubule-Associated Proteins</DescriptorName>
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<MeshHeading><DescriptorName UI="D051058" MajorTopicYN="N">Oncogene Protein v-akt</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010588" MajorTopicYN="N">Phagosomes</DescriptorName>
<QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName>
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<MeshHeading><DescriptorName UI="D060888" MajorTopicYN="N">Real-Time Polymerase Chain Reaction</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName>
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<Day>23</Day>
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<ArticleIdList><ArticleId IdType="pubmed">22355189</ArticleId>
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<ArticleId IdType="doi">10.1126/scisignal.2001931</ArticleId>
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