Solid-to-fluid–like DNA transition in viruses facilitates infection
Identifieur interne : 003823 ( Ncbi/Merge ); précédent : 003822; suivant : 003824Solid-to-fluid–like DNA transition in viruses facilitates infection
Auteurs : Ting Liu ; Udom Sae-Ueng ; Dong Li ; Gabriel C. Lander ; Xiaobing Zuo ; Bengt Jönsson [Suède] ; Donald Rau ; Ivetta Shefer ; Alex Evilevitch [Suède]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2014.
Descripteurs français
- KwdFr :
- ADN viral (), ADN viral (ultrastructure), Bactériophage lambda (), Bactériophage lambda (ultrastructure), Capside (), Cinétique, Cryomicroscopie électronique, Escherichia coli (virologie), Fluorescence, Humains, Maladies virales (virologie), Microscopie à force atomique, Thermodynamique, Transition de phase.
- MESH :
English descriptors
- KwdEn :
- Bacteriophage lambda (chemistry), Bacteriophage lambda (ultrastructure), Capsid (chemistry), Cryoelectron Microscopy, DNA, Viral (chemistry), DNA, Viral (ultrastructure), Escherichia coli (virology), Fluorescence, Humans, Kinetics, Microscopy, Atomic Force, Phase Transition, Thermodynamics, Virus Diseases (virology).
- MESH :
- chemical , chemistry : DNA, Viral.
- chemistry : Bacteriophage lambda, Capsid.
- ultrastructure : Bacteriophage lambda, DNA, Viral.
- virology : Escherichia coli, Virus Diseases.
- Cryoelectron Microscopy, Fluorescence, Humans, Kinetics, Microscopy, Atomic Force, Phase Transition, Thermodynamics.
Abstract
The efficiency of viral replication is limited by the ability of the virus to eject its genome into a cell. We discovered a fundamentally important mechanism for translocation of viral genomes into cells. For the first time, to our knowledge, we show that tightly packaged DNA in the viral capsid of a bacterial virus (phage λ) undergoes a solid-to-fluid–like structural transition that facilitates infection close to 37 °C. Our finding shows a remarkable physical adaptation of bacterial viruses to the environment of
Url:
DOI: 10.1073/pnas.1321637111
PubMed: 25271319
PubMed Central: 4205597
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PMC:4205597Le document en format XML
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and" id="aff5">Laboratory of Physical and Structural Biology, Program in Physical Biology,<institution>National Institutes of Health</institution>, Bethesda,<addr-line>MD</addr-line> 20892</nlm:aff></affiliation></author><author><name sortKey="Shefer, Ivetta" sort="Shefer, Ivetta" uniqKey="Shefer I" first="Ivetta" last="Shefer">Ivetta Shefer</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Evilevitch, Alex" sort="Evilevitch, Alex" uniqKey="Evilevitch A" first="Alex" last="Evilevitch">Alex Evilevitch</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="aff6">Department of Biochemistry and Structural Biology,<institution>Lund University</institution>, SE-221 00 Lund,<country>Sweden</country></nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteriophage lambda (chemistry)</term><term>Bacteriophage lambda (ultrastructure)</term><term>Capsid (chemistry)</term><term>Cryoelectron Microscopy</term><term>DNA, Viral (chemistry)</term><term>DNA, Viral (ultrastructure)</term><term>Escherichia coli (virology)</term><term>Fluorescence</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Atomic Force</term><term>Phase Transition</term><term>Thermodynamics</term><term>Virus Diseases (virology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN viral ()</term><term>ADN viral (ultrastructure)</term><term>Bactériophage lambda ()</term><term>Bactériophage lambda (ultrastructure)</term><term>Capside ()</term><term>Cinétique</term><term>Cryomicroscopie électronique</term><term>Escherichia coli (virologie)</term><term>Fluorescence</term><term>Humains</term><term>Maladies virales (virologie)</term><term>Microscopie à force atomique</term><term>Thermodynamique</term><term>Transition de phase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Viral</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bacteriophage lambda</term><term>Capsid</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Bacteriophage lambda</term><term>DNA, Viral</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Escherichia coli</term><term>Maladies virales</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Escherichia coli</term><term>Virus Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cryoelectron Microscopy</term><term>Fluorescence</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Atomic Force</term><term>Phase Transition</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN viral</term><term>Bactériophage lambda</term><term>Capside</term><term>Cinétique</term><term>Cryomicroscopie électronique</term><term>Fluorescence</term><term>Humains</term><term>Microscopie à force atomique</term><term>Thermodynamique</term><term>Transition de phase</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Significance</title><p>The efficiency of viral replication is limited by the ability of the virus to eject its genome into a cell. We discovered a fundamentally important mechanism for translocation of viral genomes into cells. For the first time, to our knowledge, we show that tightly packaged DNA in the viral capsid of a bacterial virus (phage λ) undergoes a solid-to-fluid–like structural transition that facilitates infection close to 37 °C. Our finding shows a remarkable physical adaptation of bacterial viruses to the environment of <italic>Escherichia coli</italic> cells in a human host.</p></div></front></TEI><double pmid="25271319"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Solid-to-fluid–like DNA transition in viruses facilitates infection</title><author><name sortKey="Liu, Ting" sort="Liu, Ting" uniqKey="Liu T" first="Ting" last="Liu">Ting Liu</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Sae Ueng, Udom" sort="Sae Ueng, Udom" uniqKey="Sae Ueng U" first="Udom" last="Sae-Ueng">Udom Sae-Ueng</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Li, Dong" sort="Li, Dong" uniqKey="Li D" first="Dong" last="Li">Dong Li</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Lander, Gabriel C" sort="Lander, Gabriel C" uniqKey="Lander G" first="Gabriel C." last="Lander">Gabriel C. Lander</name><affiliation><nlm:aff id="aff2">Department of Integrative Structural and Computational Biology,<institution>The Scripps Research Institute</institution>, La Jolla,<addr-line>CA</addr-line> 92037;</nlm:aff></affiliation></author><author><name sortKey="Zuo, Xiaobing" sort="Zuo, Xiaobing" uniqKey="Zuo X" first="Xiaobing" last="Zuo">Xiaobing Zuo</name><affiliation><nlm:aff id="aff3">X-ray Science Division, Advanced Photon Source,<institution>Argonne National Laboratory</institution>, Argonne,<addr-line>IL</addr-line> 60439;</nlm:aff></affiliation></author><author><name sortKey="Jonsson, Bengt" sort="Jonsson, Bengt" uniqKey="Jonsson B" first="Bengt" last="Jönsson">Bengt Jönsson</name><affiliation wicri:level="1"><nlm:aff id="aff4">Department of Biophysical Chemistry,<institution>Lund University</institution>, SE-221 00 Lund,<country>Sweden</country>;</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Rau, Donald" sort="Rau, Donald" uniqKey="Rau D" first="Donald" last="Rau">Donald Rau</name><affiliation><nlm:aff wicri:cut="; and" id="aff5">Laboratory of Physical and Structural Biology, Program in Physical Biology,<institution>National Institutes of Health</institution>, Bethesda,<addr-line>MD</addr-line> 20892</nlm:aff></affiliation></author><author><name sortKey="Shefer, Ivetta" sort="Shefer, Ivetta" uniqKey="Shefer I" first="Ivetta" last="Shefer">Ivetta Shefer</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Evilevitch, Alex" sort="Evilevitch, Alex" uniqKey="Evilevitch A" first="Alex" last="Evilevitch">Alex Evilevitch</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="aff6">Department of Biochemistry and Structural Biology,<institution>Lund University</institution>, SE-221 00 Lund,<country>Sweden</country></nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25271319</idno><idno type="pmc">4205597</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4205597</idno><idno type="RBID">PMC:4205597</idno><idno type="doi">10.1073/pnas.1321637111</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000C12</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000C12</idno><idno type="wicri:Area/Pmc/Curation">000B87</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000B87</idno><idno type="wicri:Area/Pmc/Checkpoint">000549</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000549</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Solid-to-fluid–like DNA transition in viruses facilitates infection</title><author><name sortKey="Liu, Ting" sort="Liu, Ting" uniqKey="Liu T" first="Ting" last="Liu">Ting Liu</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Sae Ueng, Udom" sort="Sae Ueng, Udom" uniqKey="Sae Ueng U" first="Udom" last="Sae-Ueng">Udom Sae-Ueng</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Li, Dong" sort="Li, Dong" uniqKey="Li D" first="Dong" last="Li">Dong Li</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Lander, Gabriel C" sort="Lander, Gabriel C" uniqKey="Lander G" first="Gabriel C." last="Lander">Gabriel C. Lander</name><affiliation><nlm:aff id="aff2">Department of Integrative Structural and Computational Biology,<institution>The Scripps Research Institute</institution>, La Jolla,<addr-line>CA</addr-line> 92037;</nlm:aff></affiliation></author><author><name sortKey="Zuo, Xiaobing" sort="Zuo, Xiaobing" uniqKey="Zuo X" first="Xiaobing" last="Zuo">Xiaobing Zuo</name><affiliation><nlm:aff id="aff3">X-ray Science Division, Advanced Photon Source,<institution>Argonne National Laboratory</institution>, Argonne,<addr-line>IL</addr-line> 60439;</nlm:aff></affiliation></author><author><name sortKey="Jonsson, Bengt" sort="Jonsson, Bengt" uniqKey="Jonsson B" first="Bengt" last="Jönsson">Bengt Jönsson</name><affiliation wicri:level="1"><nlm:aff id="aff4">Department of Biophysical Chemistry,<institution>Lund University</institution>, SE-221 00 Lund,<country>Sweden</country>;</nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author><author><name sortKey="Rau, Donald" sort="Rau, Donald" uniqKey="Rau D" first="Donald" last="Rau">Donald Rau</name><affiliation><nlm:aff wicri:cut="; and" id="aff5">Laboratory of Physical and Structural Biology, Program in Physical Biology,<institution>National Institutes of Health</institution>, Bethesda,<addr-line>MD</addr-line> 20892</nlm:aff></affiliation></author><author><name sortKey="Shefer, Ivetta" sort="Shefer, Ivetta" uniqKey="Shefer I" first="Ivetta" last="Shefer">Ivetta Shefer</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation></author><author><name sortKey="Evilevitch, Alex" sort="Evilevitch, Alex" uniqKey="Evilevitch A" first="Alex" last="Evilevitch">Alex Evilevitch</name><affiliation><nlm:aff id="aff1">Department of Physics,<institution>Carnegie Mellon University</institution>, Pittsburgh,<addr-line>PA</addr-line> 15213;</nlm:aff></affiliation><affiliation wicri:level="1"><nlm:aff id="aff6">Department of Biochemistry and Structural Biology,<institution>Lund University</institution>, SE-221 00 Lund,<country>Sweden</country></nlm:aff><country xml:lang="fr">Suède</country><wicri:regionArea># see nlm:aff country strict</wicri:regionArea></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><idno type="eISSN">1091-6490</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Significance</title><p>The efficiency of viral replication is limited by the ability of the virus to eject its genome into a cell. We discovered a fundamentally important mechanism for translocation of viral genomes into cells. For the first time, to our knowledge, we show that tightly packaged DNA in the viral capsid of a bacterial virus (phage λ) undergoes a solid-to-fluid–like structural transition that facilitates infection close to 37 °C. Our finding shows a remarkable physical adaptation of bacterial viruses to the environment of <italic>Escherichia coli</italic> cells in a human host.</p></div></front></TEI></pmc><pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Solid-to-fluid-like DNA transition in viruses facilitates infection.</title><author><name sortKey="Liu, Ting" sort="Liu, Ting" uniqKey="Liu T" first="Ting" last="Liu">Ting Liu</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Sae Ueng, Udom" sort="Sae Ueng, Udom" uniqKey="Sae Ueng U" first="Udom" last="Sae-Ueng">Udom Sae-Ueng</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Li, Dong" sort="Li, Dong" uniqKey="Li D" first="Dong" last="Li">Dong Li</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Lander, Gabriel C" sort="Lander, Gabriel C" uniqKey="Lander G" first="Gabriel C" last="Lander">Gabriel C. Lander</name><affiliation wicri:level="2"><nlm:affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla</wicri:cityArea></affiliation></author><author><name sortKey="Zuo, Xiaobing" sort="Zuo, Xiaobing" uniqKey="Zuo X" first="Xiaobing" last="Zuo">Xiaobing Zuo</name><affiliation wicri:level="2"><nlm:affiliation>X-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60439;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Illinois</region></placeName><wicri:cityArea>X-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne</wicri:cityArea></affiliation></author><author><name sortKey="Jonsson, Bengt" sort="Jonsson, Bengt" uniqKey="Jonsson B" first="Bengt" last="Jönsson">Bengt Jönsson</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biophysical Chemistry, Lund University, SE-221 00 Lund, Sweden;</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Biophysical Chemistry, Lund University, SE-221 00 Lund</wicri:regionArea><wicri:noRegion>SE-221 00 Lund</wicri:noRegion></affiliation></author><author><name sortKey="Rau, Donald" sort="Rau, Donald" uniqKey="Rau D" first="Donald" last="Rau">Donald Rau</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Physical and Structural Biology, Program in Physical Biology, National Institutes of Health, Bethesda, MD 20892; and.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Laboratory of Physical and Structural Biology, Program in Physical Biology, National Institutes of Health, Bethesda</wicri:cityArea></affiliation></author><author><name sortKey="Shefer, Ivetta" sort="Shefer, Ivetta" uniqKey="Shefer I" first="Ivetta" last="Shefer">Ivetta Shefer</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Evilevitch, Alex" sort="Evilevitch, Alex" uniqKey="Evilevitch A" first="Alex" last="Evilevitch">Alex Evilevitch</name><affiliation wicri:level="4"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213; Department of Biochemistry and Structural Biology, Lund University, SE-221 00 Lund, Sweden alexe@cmu.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213; Department of Biochemistry and Structural Biology, Lund University, SE-221 00 Lund</wicri:regionArea><orgName type="university">Université Carnegie-Mellon</orgName><placeName><settlement type="city">Pittsburgh</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25271319</idno><idno type="pmid">25271319</idno><idno type="doi">10.1073/pnas.1321637111</idno><idno type="wicri:Area/PubMed/Corpus">001851</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001851</idno><idno type="wicri:Area/PubMed/Curation">001843</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001843</idno><idno type="wicri:Area/PubMed/Checkpoint">001843</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001843</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Solid-to-fluid-like DNA transition in viruses facilitates infection.</title><author><name sortKey="Liu, Ting" sort="Liu, Ting" uniqKey="Liu T" first="Ting" last="Liu">Ting Liu</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Sae Ueng, Udom" sort="Sae Ueng, Udom" uniqKey="Sae Ueng U" first="Udom" last="Sae-Ueng">Udom Sae-Ueng</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Li, Dong" sort="Li, Dong" uniqKey="Li D" first="Dong" last="Li">Dong Li</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Lander, Gabriel C" sort="Lander, Gabriel C" uniqKey="Lander G" first="Gabriel C" last="Lander">Gabriel C. Lander</name><affiliation wicri:level="2"><nlm:affiliation>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Californie</region></placeName><wicri:cityArea>Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla</wicri:cityArea></affiliation></author><author><name sortKey="Zuo, Xiaobing" sort="Zuo, Xiaobing" uniqKey="Zuo X" first="Xiaobing" last="Zuo">Xiaobing Zuo</name><affiliation wicri:level="2"><nlm:affiliation>X-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne, IL 60439;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Illinois</region></placeName><wicri:cityArea>X-ray Science Division, Advanced Photon Source, Argonne National Laboratory, Argonne</wicri:cityArea></affiliation></author><author><name sortKey="Jonsson, Bengt" sort="Jonsson, Bengt" uniqKey="Jonsson B" first="Bengt" last="Jönsson">Bengt Jönsson</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biophysical Chemistry, Lund University, SE-221 00 Lund, Sweden;</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Biophysical Chemistry, Lund University, SE-221 00 Lund</wicri:regionArea><wicri:noRegion>SE-221 00 Lund</wicri:noRegion></affiliation></author><author><name sortKey="Rau, Donald" sort="Rau, Donald" uniqKey="Rau D" first="Donald" last="Rau">Donald Rau</name><affiliation wicri:level="2"><nlm:affiliation>Laboratory of Physical and Structural Biology, Program in Physical Biology, National Institutes of Health, Bethesda, MD 20892; and.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>Laboratory of Physical and Structural Biology, Program in Physical Biology, National Institutes of Health, Bethesda</wicri:cityArea></affiliation></author><author><name sortKey="Shefer, Ivetta" sort="Shefer, Ivetta" uniqKey="Shefer I" first="Ivetta" last="Shefer">Ivetta Shefer</name><affiliation wicri:level="2"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213;</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Pennsylvanie</region></placeName><wicri:cityArea>Department of Physics, Carnegie Mellon University, Pittsburgh</wicri:cityArea></affiliation></author><author><name sortKey="Evilevitch, Alex" sort="Evilevitch, Alex" uniqKey="Evilevitch A" first="Alex" last="Evilevitch">Alex Evilevitch</name><affiliation wicri:level="4"><nlm:affiliation>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213; Department of Biochemistry and Structural Biology, Lund University, SE-221 00 Lund, Sweden alexe@cmu.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Physics, Carnegie Mellon University, Pittsburgh, PA 15213; Department of Biochemistry and Structural Biology, Lund University, SE-221 00 Lund</wicri:regionArea><orgName type="university">Université Carnegie-Mellon</orgName><placeName><settlement type="city">Pittsburgh</settlement><region type="state">Pennsylvanie</region></placeName></affiliation></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacteriophage lambda (chemistry)</term><term>Bacteriophage lambda (ultrastructure)</term><term>Capsid (chemistry)</term><term>Cryoelectron Microscopy</term><term>DNA, Viral (chemistry)</term><term>DNA, Viral (ultrastructure)</term><term>Escherichia coli (virology)</term><term>Fluorescence</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Atomic Force</term><term>Phase Transition</term><term>Thermodynamics</term><term>Virus Diseases (virology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>ADN viral ()</term><term>ADN viral (ultrastructure)</term><term>Bactériophage lambda ()</term><term>Bactériophage lambda (ultrastructure)</term><term>Capside ()</term><term>Cinétique</term><term>Cryomicroscopie électronique</term><term>Escherichia coli (virologie)</term><term>Fluorescence</term><term>Humains</term><term>Maladies virales (virologie)</term><term>Microscopie à force atomique</term><term>Thermodynamique</term><term>Transition de phase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>DNA, Viral</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bacteriophage lambda</term><term>Capsid</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Bacteriophage lambda</term><term>DNA, Viral</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Escherichia coli</term><term>Maladies virales</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Escherichia coli</term><term>Virus Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cryoelectron Microscopy</term><term>Fluorescence</term><term>Humans</term><term>Kinetics</term><term>Microscopy, Atomic Force</term><term>Phase Transition</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>ADN viral</term><term>Bactériophage lambda</term><term>Capside</term><term>Cinétique</term><term>Cryomicroscopie électronique</term><term>Fluorescence</term><term>Humains</term><term>Microscopie à force atomique</term><term>Thermodynamique</term><term>Transition de phase</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Releasing the packaged viral DNA into the host cell is an essential process to initiate viral infection. In many double-stranded DNA bacterial viruses and herpesviruses, the tightly packaged genome is hexagonally ordered and stressed in the protein shell, called the capsid. DNA condensed in this state inside viral capsids has been shown to be trapped in a glassy state, with restricted molecular motion in vitro. This limited intracapsid DNA mobility is caused by the sliding friction between closely packaged DNA strands, as a result of the repulsive interactions between the negative charges on the DNA helices. It had been unclear how this rigid crystalline structure of the viral genome rapidly ejects from the capsid, reaching rates of 60,000 bp/s. Through a combination of single-molecule and bulk techniques, we determined how the structure and energy of the encapsidated DNA in phage λ regulates the mobility required for its ejection. Our data show that packaged λ-DNA undergoes a solid-to-fluid-like disordering transition as a function of temperature, resulting locally in less densely packed DNA, reducing DNA-DNA repulsions. This process leads to a significant increase in genome mobility or fluidity, which facilitates genome release at temperatures close to that of viral infection (37 °C), suggesting a remarkable physical adaptation of bacterial viruses to the environment of Escherichia coli cells in a human host.</div></front></TEI></pubmed></double></record>Pour manipuler ce document sous Unix (Dilib)
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