Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization.
Identifieur interne : 002E43 ( PubMed/Curation ); précédent : 002E42; suivant : 002E44Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization.
Auteurs : Elaine Chiu [Nouvelle-Zélande] ; Marcel Hijnen [Australie] ; Richard D. Bunker [Nouvelle-Zélande] ; Marion Boudes [Australie] ; Chitra Rajendran [Suisse] ; Kaheina Aizel [Australie] ; Vincent Oliéric [Suisse] ; Clemens Schulze-Briese [Suisse] ; Wataru Mitsuhashi [Japon] ; Vivienne Young ; Vernon K. Ward ; Max Bergoin [France] ; Peter Metcalf [États-Unis] ; Fasséli Coulibaly [États-Unis]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux, Chitine (), Cristallisation, Cristallographie aux rayons X, Disulfures (), Domaine catalytique, Données de séquences moléculaires, Facteurs de virulence (), Facteurs de virulence (physiologie), Insectes, Insecticides (), Mixed function oxygenases (), Modèles moléculaires, Oxygène (), Oxygénases (), Polyosides, Poxviridae (métabolisme), Protéines virales (), Structure tertiaire des protéines, Structures macromoléculaires, Séquence d'acides aminés, Virulence, Virus ().
- MESH :
- métabolisme : Poxviridae.
- physiologie : Facteurs de virulence.
- Animaux, Chitine, Cristallisation, Cristallographie aux rayons X, Disulfures, Domaine catalytique, Données de séquences moléculaires, Facteurs de virulence, Insectes, Insecticides, Mixed function oxygenases, Modèles moléculaires, Oxygène, Oxygénases, Polyosides, Protéines virales, Structure tertiaire des protéines, Structures macromoléculaires, Séquence d'acides aminés, Virulence, Virus.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Catalytic Domain, Chitin (chemistry), Crystallization, Crystallography, X-Ray, Disulfides (chemistry), Insecticides (chemistry), Insects, Macromolecular Substances, Mixed Function Oxygenases (chemistry), Models, Molecular, Molecular Sequence Data, Oxygen (chemistry), Oxygenases (chemistry), Polysaccharides, Poxviridae (metabolism), Protein Structure, Tertiary, Viral Proteins (chemistry), Virulence, Virulence Factors (chemistry), Virulence Factors (physiology), Viruses (chemistry).
- MESH :
- chemical , chemistry : Chitin, Disulfides, Insecticides, Mixed Function Oxygenases, Oxygen, Oxygenases, Viral Proteins, Virulence Factors.
- chemistry : Viruses.
- metabolism : Poxviridae.
- chemical , physiology : Virulence Factors.
- Amino Acid Sequence, Animals, Catalytic Domain, Crystallization, Crystallography, X-Ray, Insects, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, Polysaccharides, Protein Structure, Tertiary, Virulence.
Abstract
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.
DOI: 10.1073/pnas.1418798112
PubMed: 25787255
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Vivienne Young<affiliation><nlm:affiliation>Department of Microbiology and Immunology, School of Medical Sciences, University of Otago, Dunedin, 9054, New Zealand; and.</nlm:affiliation><wicri:noCountry code="subField">New Zealand; and</wicri:noCountry></affiliation><affiliation><nlm:affiliation>Department of Microbiology and Immunology, School of Medical Sciences, University of Otago, Dunedin, 9054, New Zealand; and.</nlm:affiliation><wicri:noCountry code="subField">New Zealand; and</wicri:noCountry></affiliation>Le document en format XML
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Ward</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, School of Medical Sciences, University of Otago, Dunedin, 9054, New Zealand; and.</nlm:affiliation><wicri:noCountry code="subField">New Zealand; and</wicri:noCountry></affiliation></author><author><name sortKey="Bergoin, Max" sort="Bergoin, Max" uniqKey="Bergoin M" first="Max" last="Bergoin">Max Bergoin</name><affiliation wicri:level="1"><nlm:affiliation>Université Montpellier 2, Montpellier 34095, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Université Montpellier 2, Montpellier 34095</wicri:regionArea></affiliation></author><author><name sortKey="Metcalf, Peter" sort="Metcalf, Peter" uniqKey="Metcalf P" first="Peter" last="Metcalf">Peter Metcalf</name><affiliation wicri:level="1"><nlm:affiliation>School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand; fasseli.coulibaly@monash.edu peter.metcalf@auckland.ac.nz.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>School of Biological Sciences, University of Auckland, Auckland, 1010</wicri:regionArea></affiliation></author><author><name sortKey="Coulibaly, Fasseli" sort="Coulibaly, Fasseli" uniqKey="Coulibaly F" first="Fasséli" last="Coulibaly">Fasséli Coulibaly</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia; fasseli.coulibaly@monash.edu peter.metcalf@auckland.ac.nz.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800</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="eISSN">1091-6490</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Catalytic Domain</term><term>Chitin (chemistry)</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Disulfides (chemistry)</term><term>Insecticides (chemistry)</term><term>Insects</term><term>Macromolecular Substances</term><term>Mixed Function Oxygenases (chemistry)</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Oxygen (chemistry)</term><term>Oxygenases (chemistry)</term><term>Polysaccharides</term><term>Poxviridae (metabolism)</term><term>Protein Structure, Tertiary</term><term>Viral Proteins (chemistry)</term><term>Virulence</term><term>Virulence Factors (chemistry)</term><term>Virulence Factors (physiology)</term><term>Viruses (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Chitine ()</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Disulfures ()</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Facteurs de virulence ()</term><term>Facteurs de virulence (physiologie)</term><term>Insectes</term><term>Insecticides ()</term><term>Mixed function oxygenases ()</term><term>Modèles moléculaires</term><term>Oxygène ()</term><term>Oxygénases ()</term><term>Polyosides</term><term>Poxviridae (métabolisme)</term><term>Protéines virales ()</term><term>Structure tertiaire des protéines</term><term>Structures macromoléculaires</term><term>Séquence d'acides aminés</term><term>Virulence</term><term>Virus ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Chitin</term><term>Disulfides</term><term>Insecticides</term><term>Mixed Function Oxygenases</term><term>Oxygen</term><term>Oxygenases</term><term>Viral Proteins</term><term>Virulence Factors</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Viruses</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Poxviridae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Poxviridae</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Facteurs de virulence</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Virulence Factors</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Catalytic Domain</term><term>Crystallization</term><term>Crystallography, X-Ray</term><term>Insects</term><term>Macromolecular Substances</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Polysaccharides</term><term>Protein Structure, Tertiary</term><term>Virulence</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Chitine</term><term>Cristallisation</term><term>Cristallographie aux rayons X</term><term>Disulfures</term><term>Domaine catalytique</term><term>Données de séquences moléculaires</term><term>Facteurs de virulence</term><term>Insectes</term><term>Insecticides</term><term>Mixed function oxygenases</term><term>Modèles moléculaires</term><term>Oxygène</term><term>Oxygénases</term><term>Polyosides</term><term>Protéines virales</term><term>Structure tertiaire des protéines</term><term>Structures macromoléculaires</term><term>Séquence d'acides aminés</term><term>Virulence</term><term>Virus</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25787255</PMID><DateCreated><Year>2015</Year><Month>04</Month><Day>01</Day></DateCreated><DateCompleted><Year>2015</Year><Month>06</Month><Day>22</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>112</Volume><Issue>13</Issue><PubDate><Year>2015</Year><Month>Mar</Month><Day>31</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Structural basis for the enhancement of virulence by viral spindles and their in vivo crystallization.</ArticleTitle><Pagination><MedlinePgn>3973-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1418798112</ELocationID><Abstract><AbstractText>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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chiu</LastName><ForeName>Elaine</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hijnen</LastName><ForeName>Marcel</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bunker</LastName><ForeName>Richard D</ForeName><Initials>RD</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Boudes</LastName><ForeName>Marion</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rajendran</LastName><ForeName>Chitra</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Swiss Light Source at Paul Scherrer Institut, 5232 Villigen, Switzerland;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aizel</LastName><ForeName>Kaheina</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Oliéric</LastName><ForeName>Vincent</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Swiss Light Source at Paul Scherrer Institut, 5232 Villigen, Switzerland;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schulze-Briese</LastName><ForeName>Clemens</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Swiss Light Source at Paul Scherrer Institut, 5232 Villigen, Switzerland;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mitsuhashi</LastName><ForeName>Wataru</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>National Institute of Agrobiological Sciences, Tsukuba, Ibaraki 305-8634, Japan;</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Young</LastName><ForeName>Vivienne</ForeName><Initials>V</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, School of Medical Sciences, University of Otago, Dunedin, 9054, New Zealand; and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ward</LastName><ForeName>Vernon K</ForeName><Initials>VK</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, School of Medical Sciences, University of Otago, Dunedin, 9054, New Zealand; and.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bergoin</LastName><ForeName>Max</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Université Montpellier 2, Montpellier 34095, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Metcalf</LastName><ForeName>Peter</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand; fasseli.coulibaly@monash.edu peter.metcalf@auckland.ac.nz.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coulibaly</LastName><ForeName>Fasséli</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biology, School of Biomedical Sciences, Monash University, Clayton, VIC 3800, Australia; fasseli.coulibaly@monash.edu peter.metcalf@auckland.ac.nz.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><DataBankList CompleteYN="Y"><DataBank><DataBankName>PDB</DataBankName><AccessionNumberList><AccessionNumber>4OW5</AccessionNumber><AccessionNumber>4X27</AccessionNumber><AccessionNumber>4X29</AccessionNumber><AccessionNumber>4YN1</AccessionNumber><AccessionNumber>4YN2</AccessionNumber></AccessionNumberList></DataBank></DataBankList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2015</Year><Month>03</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007306">Insecticides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D046911">Macromolecular Substances</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011134">Polysaccharides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D037521">Virulence Factors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C093475">fusolin protein, entomopoxvirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>1398-61-4</RegistryNumber><NameOfSubstance UI="D002686">Chitin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D006899">Mixed Function Oxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.13.-</RegistryNumber><NameOfSubstance UI="D010105">Oxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>S88TT14065</RegistryNumber><NameOfSubstance UI="D010100">Oxygen</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Virus Res. 2003 Oct;96(1-2):113-22</RefSource><PMID Version="1">12951271</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Struct Funct Genomics. 2012 Jun;13(2):81-90</RefSource><PMID Version="1">22418934</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>J Virol. 2008 Dec;82(24):12406-15</RefSource><PMID Version="1">18829750</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Acta Crystallogr D Biol Crystallogr. 2010 Apr;66(Pt 4):486-501</RefSource><PMID 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MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007306" MajorTopicYN="N">Insecticides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007313" MajorTopicYN="N">Insects</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D046911" MajorTopicYN="N">Macromolecular Substances</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006899" MajorTopicYN="N">Mixed Function Oxygenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010100" MajorTopicYN="N">Oxygen</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010105" MajorTopicYN="N">Oxygenases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011134" MajorTopicYN="N">Polysaccharides</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011212" MajorTopicYN="N">Poxviridae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014774" MajorTopicYN="N">Virulence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D037521" MajorTopicYN="N">Virulence Factors</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014780" MajorTopicYN="N">Viruses</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading></MeshHeadingList><OtherID Source="NLM">PMC4386404</OtherID><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">LPMO</Keyword><Keyword MajorTopicYN="N">in vivo crystallization</Keyword><Keyword MajorTopicYN="N">microcrystallography</Keyword><Keyword MajorTopicYN="N">pesticide</Keyword><Keyword MajorTopicYN="N">poxvirus</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2015</Year><Month>3</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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