Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization
Identifieur interne : 001C03 ( Pmc/Corpus ); précédent : 001C02; suivant : 001C04Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization
Auteurs : Elaine Chiu ; Marcel Hijnen ; Richard D. Bunker ; Marion Boudes ; Chitra Rajendran ; Kaheina Aizel ; Vincent Oliéric ; Clemens Schulze-Briese ; Wataru Mitsuhashi ; Vivienne Young ; Vernon K. Ward ; Max Bergoin ; Peter Metcalf ; Fasséli CoulibalySource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2015.
Abstract
X-ray crystallography is a powerful approach for understanding the structure and function of biological macromolecules but is largely limited to molecules that form high-quality crystals in the laboratory. Here we present the structure of protein crystals that form naturally in virally infected insects and boost the insecticidal activity of oral pathogens. By proposing a mode of action for these virulence factors based on enzymes degrading chitin by oxidation, our findings may guide their use as synergetic additives to common bioinsecticides. They also reveal that these proteins assemble into ultra-stable crystals stabilized by a 3D network of covalent bonds, a unique strategy for achieving efficient protein crystallization in the complex environment of the cell.
Url:
DOI: 10.1073/pnas.1418798112
PubMed: 25787255
PubMed Central: 4386404
Links to Exploration step
PMC:4386404Le document en format XML
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Bunker</name><affiliation><nlm:aff id="aff1">School of Biological Sciences,<institution>University of Auckland</institution>, Auckland,<country>1010, New Zealand</country>;</nlm:aff></affiliation></author><author><name sortKey="Boudes, Marion" sort="Boudes, Marion" uniqKey="Boudes M" first="Marion" last="Boudes">Marion Boudes</name><affiliation><nlm:aff id="aff2">Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Rajendran, Chitra" sort="Rajendran, Chitra" uniqKey="Rajendran C" first="Chitra" last="Rajendran">Chitra Rajendran</name><affiliation><nlm:aff id="aff3"><institution>Swiss Light Source at Paul Scherrer Institut</institution>, 5232 Villigen,<country>Switzerland</country>;</nlm:aff></affiliation></author><author><name sortKey="Aizel, Kaheina" sort="Aizel, Kaheina" uniqKey="Aizel K" first="Kaheina" last="Aizel">Kaheina Aizel</name><affiliation><nlm:aff id="aff2">Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Olieric, Vincent" sort="Olieric, Vincent" uniqKey="Olieric V" first="Vincent" last="Oliéric">Vincent Oliéric</name><affiliation><nlm:aff id="aff3"><institution>Swiss Light Source at Paul Scherrer Institut</institution>, 5232 Villigen,<country>Switzerland</country>;</nlm:aff></affiliation></author><author><name sortKey="Schulze Briese, Clemens" sort="Schulze Briese, Clemens" uniqKey="Schulze Briese C" first="Clemens" last="Schulze-Briese">Clemens Schulze-Briese</name><affiliation><nlm:aff id="aff3"><institution>Swiss Light Source at Paul Scherrer Institut</institution>, 5232 Villigen,<country>Switzerland</country>;</nlm:aff></affiliation></author><author><name sortKey="Mitsuhashi, Wataru" sort="Mitsuhashi, Wataru" uniqKey="Mitsuhashi W" first="Wataru" last="Mitsuhashi">Wataru Mitsuhashi</name><affiliation><nlm:aff id="aff4"><institution>National Institute of Agrobiological Sciences</institution>, Tsukuba, Ibaraki 305-8634,<country>Japan</country>;</nlm:aff></affiliation></author><author><name sortKey="Young, Vivienne" sort="Young, Vivienne" uniqKey="Young V" first="Vivienne" last="Young">Vivienne Young</name><affiliation><nlm:aff wicri:cut="; and" id="aff5">Department of Microbiology and Immunology, School of Medical Sciences,<institution>University of Otago</institution>, Dunedin,<country>9054, New Zealand</country></nlm:aff></affiliation></author><author><name sortKey="Ward, Vernon K" sort="Ward, Vernon K" uniqKey="Ward V" first="Vernon K." last="Ward">Vernon K. Ward</name><affiliation><nlm:aff wicri:cut="; and" id="aff5">Department of Microbiology and Immunology, School of Medical Sciences,<institution>University of Otago</institution>, Dunedin,<country>9054, New Zealand</country></nlm:aff></affiliation></author><author><name sortKey="Bergoin, Max" sort="Bergoin, Max" uniqKey="Bergoin M" first="Max" last="Bergoin">Max Bergoin</name><affiliation><nlm:aff id="aff6"><institution>Université Montpellier 2</institution>,<country>Montpellier 34095, France</country></nlm:aff></affiliation></author><author><name sortKey="Metcalf, Peter" sort="Metcalf, Peter" uniqKey="Metcalf P" first="Peter" last="Metcalf">Peter Metcalf</name><affiliation><nlm:aff id="aff1">School of Biological Sciences,<institution>University of Auckland</institution>, Auckland,<country>1010, New Zealand</country>;</nlm:aff></affiliation></author><author><name sortKey="Coulibaly, Fasseli" sort="Coulibaly, Fasseli" uniqKey="Coulibaly F" first="Fasséli" last="Coulibaly">Fasséli Coulibaly</name><affiliation><nlm:aff id="aff2">Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25787255</idno><idno type="pmc">4386404</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4386404</idno><idno type="RBID">PMC:4386404</idno><idno type="doi">10.1073/pnas.1418798112</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">001C03</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001C03</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization</title><author><name sortKey="Chiu, Elaine" sort="Chiu, Elaine" uniqKey="Chiu E" first="Elaine" last="Chiu">Elaine Chiu</name><affiliation><nlm:aff id="aff1">School of Biological Sciences,<institution>University of Auckland</institution>, Auckland,<country>1010, New Zealand</country>;</nlm:aff></affiliation></author><author><name sortKey="Hijnen, Marcel" sort="Hijnen, Marcel" uniqKey="Hijnen M" first="Marcel" last="Hijnen">Marcel Hijnen</name><affiliation><nlm:aff id="aff2">Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Bunker, Richard D" sort="Bunker, Richard D" uniqKey="Bunker R" first="Richard D." last="Bunker">Richard D. Bunker</name><affiliation><nlm:aff id="aff1">School of Biological Sciences,<institution>University of Auckland</institution>, Auckland,<country>1010, New Zealand</country>;</nlm:aff></affiliation></author><author><name sortKey="Boudes, Marion" sort="Boudes, Marion" uniqKey="Boudes M" first="Marion" last="Boudes">Marion Boudes</name><affiliation><nlm:aff id="aff2">Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Rajendran, Chitra" sort="Rajendran, Chitra" uniqKey="Rajendran C" first="Chitra" last="Rajendran">Chitra Rajendran</name><affiliation><nlm:aff id="aff3"><institution>Swiss Light Source at Paul Scherrer Institut</institution>, 5232 Villigen,<country>Switzerland</country>;</nlm:aff></affiliation></author><author><name sortKey="Aizel, Kaheina" sort="Aizel, Kaheina" uniqKey="Aizel K" first="Kaheina" last="Aizel">Kaheina Aizel</name><affiliation><nlm:aff id="aff2">Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</nlm:aff></affiliation></author><author><name sortKey="Olieric, Vincent" sort="Olieric, Vincent" uniqKey="Olieric V" first="Vincent" last="Oliéric">Vincent Oliéric</name><affiliation><nlm:aff id="aff3"><institution>Swiss Light Source at Paul Scherrer Institut</institution>, 5232 Villigen,<country>Switzerland</country>;</nlm:aff></affiliation></author><author><name sortKey="Schulze Briese, Clemens" sort="Schulze Briese, Clemens" uniqKey="Schulze Briese C" first="Clemens" last="Schulze-Briese">Clemens Schulze-Briese</name><affiliation><nlm:aff id="aff3"><institution>Swiss Light Source at Paul Scherrer Institut</institution>, 5232 Villigen,<country>Switzerland</country>;</nlm:aff></affiliation></author><author><name sortKey="Mitsuhashi, Wataru" sort="Mitsuhashi, Wataru" uniqKey="Mitsuhashi W" first="Wataru" last="Mitsuhashi">Wataru Mitsuhashi</name><affiliation><nlm:aff id="aff4"><institution>National Institute of Agrobiological Sciences</institution>, Tsukuba, Ibaraki 305-8634,<country>Japan</country>;</nlm:aff></affiliation></author><author><name sortKey="Young, Vivienne" sort="Young, Vivienne" uniqKey="Young V" first="Vivienne" last="Young">Vivienne Young</name><affiliation><nlm:aff wicri:cut="; and" id="aff5">Department of Microbiology and Immunology, School of Medical Sciences,<institution>University of Otago</institution>, Dunedin,<country>9054, New Zealand</country></nlm:aff></affiliation></author><author><name sortKey="Ward, Vernon K" sort="Ward, Vernon K" uniqKey="Ward V" first="Vernon K." last="Ward">Vernon K. Ward</name><affiliation><nlm:aff wicri:cut="; and" id="aff5">Department of Microbiology and Immunology, School of Medical Sciences,<institution>University of Otago</institution>, Dunedin,<country>9054, New Zealand</country></nlm:aff></affiliation></author><author><name sortKey="Bergoin, Max" sort="Bergoin, Max" uniqKey="Bergoin M" first="Max" last="Bergoin">Max Bergoin</name><affiliation><nlm:aff id="aff6"><institution>Université Montpellier 2</institution>,<country>Montpellier 34095, France</country></nlm:aff></affiliation></author><author><name sortKey="Metcalf, Peter" sort="Metcalf, Peter" uniqKey="Metcalf P" first="Peter" last="Metcalf">Peter Metcalf</name><affiliation><nlm:aff id="aff1">School of Biological Sciences,<institution>University of Auckland</institution>, Auckland,<country>1010, New Zealand</country>;</nlm:aff></affiliation></author><author><name sortKey="Coulibaly, Fasseli" sort="Coulibaly, Fasseli" uniqKey="Coulibaly F" first="Fasséli" last="Coulibaly">Fasséli Coulibaly</name><affiliation><nlm:aff id="aff2">Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</nlm:aff></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="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Significance</title><p>X-ray crystallography is a powerful approach for understanding the structure and function of biological macromolecules but is largely limited to molecules that form high-quality crystals in the laboratory. Here we present the structure of protein crystals that form naturally in virally infected insects and boost the insecticidal activity of oral pathogens. By proposing a mode of action for these virulence factors based on enzymes degrading chitin by oxidation, our findings may guide their use as synergetic additives to common bioinsecticides. They also reveal that these proteins assemble into ultra-stable crystals stabilized by a 3D network of covalent bonds, a unique strategy for achieving efficient protein crystallization in the complex environment of the cell.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Proc Natl Acad Sci U S A</journal-id><journal-id journal-id-type="iso-abbrev">Proc. Natl. Acad. Sci. U.S.A</journal-id><journal-id journal-id-type="hwp">pnas</journal-id><journal-id journal-id-type="pmc">pnas</journal-id><journal-id journal-id-type="publisher-id">PNAS</journal-id><journal-title-group><journal-title>Proceedings of the National Academy of Sciences of the United States of America</journal-title></journal-title-group><issn pub-type="ppub">0027-8424</issn><issn pub-type="epub">1091-6490</issn><publisher><publisher-name>National Academy of Sciences</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25787255</article-id><article-id pub-id-type="pmc">4386404</article-id><article-id pub-id-type="publisher-id">201418798</article-id><article-id pub-id-type="doi">10.1073/pnas.1418798112</article-id><article-categories><subj-group subj-group-type="heading"><subject>Biological Sciences</subject><subj-group><subject>Biochemistry</subject></subj-group></subj-group></article-categories><title-group><article-title>Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization</article-title><alt-title alt-title-type="short">Structure of viral spindles</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Chiu</surname><given-names>Elaine</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Hijnen</surname><given-names>Marcel</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="author-notes" rid="fn1"><sup>1</sup></xref><xref ref-type="author-notes" rid="fn2"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bunker</surname><given-names>Richard D.</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="author-notes" rid="fn3"><sup>3</sup></xref></contrib><contrib contrib-type="author"><name><surname>Boudes</surname><given-names>Marion</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Rajendran</surname><given-names>Chitra</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref><xref ref-type="author-notes" rid="fn4"><sup>4</sup></xref></contrib><contrib contrib-type="author"><name><surname>Aizel</surname><given-names>Kaheina</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref></contrib><contrib contrib-type="author"><name><surname>Oliéric</surname><given-names>Vincent</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref></contrib><contrib contrib-type="author"><name><surname>Schulze-Briese</surname><given-names>Clemens</given-names></name><xref ref-type="aff" rid="aff3"><sup>c</sup></xref><xref ref-type="author-notes" rid="fn5"><sup>5</sup></xref></contrib><contrib contrib-type="author"><name><surname>Mitsuhashi</surname><given-names>Wataru</given-names></name><xref ref-type="aff" rid="aff4"><sup>d</sup></xref></contrib><contrib contrib-type="author"><name><surname>Young</surname><given-names>Vivienne</given-names></name><xref ref-type="aff" rid="aff5"><sup>e</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ward</surname><given-names>Vernon K.</given-names></name><xref ref-type="aff" rid="aff5"><sup>e</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bergoin</surname><given-names>Max</given-names></name><xref ref-type="aff" rid="aff6"><sup>f</sup></xref></contrib><contrib contrib-type="author"><name><surname>Metcalf</surname><given-names>Peter</given-names></name><xref ref-type="aff" rid="aff1"><sup>a</sup></xref><xref ref-type="corresp" rid="cor1"><sup>6</sup></xref></contrib><contrib contrib-type="author"><name><surname>Coulibaly</surname><given-names>Fasséli</given-names></name><xref ref-type="aff" rid="aff2"><sup>b</sup></xref><xref ref-type="corresp" rid="cor1"><sup>6</sup></xref></contrib><aff id="aff1"><sup>a</sup>School of Biological Sciences,<institution>University of Auckland</institution>, Auckland,<country>1010, New Zealand</country>;</aff><aff id="aff2"><sup>b</sup>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences,<institution>Monash University</institution>, Clayton, VIC 3800,<country>Australia</country>;</aff><aff id="aff3"><sup>c</sup><institution>Swiss Light Source at Paul Scherrer Institut</institution>, 5232 Villigen,<country>Switzerland</country>;</aff><aff id="aff4"><sup>d</sup><institution>National Institute of Agrobiological Sciences</institution>, Tsukuba, Ibaraki 305-8634,<country>Japan</country>;</aff><aff id="aff5"><sup>e</sup>Department of Microbiology and Immunology, School of Medical Sciences,<institution>University of Otago</institution>, Dunedin,<country>9054, New Zealand</country>; and</aff><aff id="aff6"><sup>f</sup><institution>Université Montpellier 2</institution>,<country>Montpellier 34095, France</country></aff></contrib-group><author-notes><corresp id="cor1"><sup>6</sup>To whom correspondence may be addressed. Email: <email>fasseli.coulibaly@monash.edu</email> or <email>peter.metcalf@auckland.ac.nz</email>.</corresp><fn fn-type="edited-by"><p>Edited by Stephen C. Harrison, Children's Hospital, Harvard Medical School and Howard Hughes Medical Institute, Boston, MA, and approved February 24, 2015 (received for review September 30, 2014)</p></fn><fn fn-type="con"><p>Author contributions: V.K.W., P.M., and F.C. designed research; E.C., M.H., R.D.B., M. Boudes, C.R., K.A., V.O., W.M., V.Y., M. Bergoin, and F.C. performed research; W.M., V.K.W., and M. Bergoin contributed new reagents/analytic tools; E.C., M.H., R.D.B., M. Boudes, K.A., C.S.-B., and F.C. analyzed data; and V.K.W., P.M., and F.C. wrote the paper.</p></fn><fn fn-type="present-address" id="fn2"><p><sup>2</sup>Present address: GE Healthcare, Richmond, VIC 3121, Australia.</p></fn><fn fn-type="present-address" id="fn3"><p><sup>3</sup>Present address: Friedrich Miescher Institute for Biomedical Research, 4058 Basel, Switzerland.</p></fn><fn fn-type="present-address" id="fn4"><p><sup>4</sup>Present address: Department of Structural Biology, Institut fur Biophysik und Physikalische Biochemie, University of Regensburg, 93053 Regensburg, Germany.</p></fn><fn fn-type="present-address" id="fn5"><p><sup>5</sup>Present address: DECTRIS Ltd., Baden, Switzerland.</p></fn><fn fn-type="equal" id="fn1"><p><sup>1</sup>E.C. and M.H. contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>31</day><month>3</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>18</day><month>3</month><year>2015</year></pub-date><volume>112</volume><issue>13</issue><fpage>3973</fpage><lpage>3978</lpage><self-uri xlink:title="pdf" xlink:href="pnas.201418798.pdf"></self-uri><abstract abstract-type="executive-summary"><title>Significance</title><p>X-ray crystallography is a powerful approach for understanding the structure and function of biological macromolecules but is largely limited to molecules that form high-quality crystals in the laboratory. Here we present the structure of protein crystals that form naturally in virally infected insects and boost the insecticidal activity of oral pathogens. By proposing a mode of action for these virulence factors based on enzymes degrading chitin by oxidation, our findings may guide their use as synergetic additives to common bioinsecticides. They also reveal that these proteins assemble into ultra-stable crystals stabilized by a 3D network of covalent bonds, a unique strategy for achieving efficient protein crystallization in the complex environment of the cell.</p></abstract><abstract><p>The great benefits that chemical pesticides have brought to agriculture are partly offset by widespread environmental damage to nontarget species and threats to human health. Microbial bioinsecticides are considered safe and highly specific alternatives but generally lack potency. Spindles produced by insect poxviruses are crystals of the fusolin protein that considerably boost not only the virulence of these viruses but also, in cofeeding experiments, the insecticidal activity of unrelated pathogens. However, the mechanisms by which spindles assemble into ultra-stable crystals and enhance virulence are unknown. Here we describe the structure of viral spindles determined by X-ray microcrystallography from in vivo crystals purified from infected insects. We found that a C-terminal molecular arm of fusolin mediates the assembly of a globular domain, which has the hallmarks of lytic polysaccharide monooxygenases of chitinovorous bacteria. Explaining their unique stability, a 3D network of disulfide bonds between fusolin dimers covalently crosslinks the entire crystalline matrix of spindles. However, upon ingestion by a new host, removal of the molecular arm abolishes this stabilizing network leading to the dissolution of spindles. The released monooxygenase domain is then free to disrupt the chitin-rich peritrophic matrix that protects insects against oral infections. The mode of action revealed here may guide the design of potent spindles as synergetic additives to bioinsecticides.</p></abstract><kwd-group><kwd>microcrystallography</kwd><kwd>in vivo crystallization</kwd><kwd>poxvirus</kwd><kwd>LPMO</kwd><kwd>pesticide</kwd></kwd-group><funding-group><award-group id="gs1"><funding-source id="sp1">Department of Industry, Innovation, Science, Research and Tertiary Education, Australian Government | Australian Research Council (ARC)<named-content content-type="funder-id">501100000923</named-content></funding-source><award-id rid="sp1">FT1210893</award-id></award-group><award-group id="gs2"><funding-source id="sp2">Department of Industry, Innovation, Science, Research and Tertiary Education, Australian Government | Australian Research Council (ARC)<named-content content-type="funder-id">501100000923</named-content></funding-source><award-id rid="sp2">DP1314885</award-id></award-group><award-group id="gs3"><funding-source id="sp3">Royal Society of New Zealand<named-content content-type="funder-id">501100001509</named-content></funding-source><award-id rid="sp3">Marsden</award-id></award-group></funding-group><counts><page-count count="6"></page-count></counts></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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