Biomedical Applications of Lumazine Synthase.
Identifieur interne : 000903 ( PubMed/Corpus ); précédent : 000902; suivant : 000904Biomedical Applications of Lumazine Synthase.
Auteurs : Yangjie Wei ; Prashant Kumar ; Newton Wahome ; Nicholas J. Mantis ; C Russell MiddaughSource :
- Journal of pharmaceutical sciences [ 1520-6017 ] ; 2018.
English descriptors
- KwdEn :
- Animals, Drug Delivery Systems (methods), Drug Delivery Systems (trends), Humans, Immunogenicity, Vaccine (immunology), Multienzyme Complexes (administration & dosage), Multienzyme Complexes (chemistry), Multienzyme Complexes (immunology), Protein Structure, Secondary, Riboflavin Synthase (administration & dosage), Riboflavin Synthase (chemistry), Riboflavin Synthase (immunology).
- MESH :
- chemical , administration & dosage : Multienzyme Complexes, Riboflavin Synthase.
- chemical , chemistry : Multienzyme Complexes, Riboflavin Synthase.
- immunology : Immunogenicity, Vaccine, Multienzyme Complexes, Riboflavin Synthase.
- methods : Drug Delivery Systems.
- trends : Drug Delivery Systems.
- Animals, Humans, Protein Structure, Secondary.
Abstract
Lumazine synthase (LS) is a family of enzyme involved in the penultimate step in the biosynthesis of riboflavin. Its enzymatic mechanism has been well defined, and many LS structures have been solved using X-ray crystallography or cryoelectron microscopy. LS is composed of homooligomers, which vary in size and subunit number, including pentamers, decamers, and icosahedral sixty-mers, depending on its species of origin. Research on LS has expanded beyond the initial focus on its enzymatic function to properties related to its oligomeric structure and exceptional conformational stability. These attributes of LS systems have now been repurposed for use in various biomedical fields. This review primarily focuses on the applications of LS as a flexible vaccine presentation system. Presentation of antigens on the surface of LS results in a high local concentration of antigens displayed in an ordered array. Such repetitive structures enable the cross-linking of B-cell receptors and result in strong immune responses through an avidity effect. Potential issues with the use of this system and corresponding solutions are also discussed with the objective of improved utilization of the LS system in vaccine development.
DOI: 10.1016/j.xphs.2018.05.002
PubMed: 29763607
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Biomedical Applications of Lumazine Synthase.</title><author><name sortKey="Wei, Yangjie" sort="Wei, Yangjie" uniqKey="Wei Y" first="Yangjie" last="Wei">Yangjie Wei</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</nlm:affiliation></affiliation></author><author><name sortKey="Kumar, Prashant" sort="Kumar, Prashant" uniqKey="Kumar P" first="Prashant" last="Kumar">Prashant Kumar</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</nlm:affiliation></affiliation></author><author><name sortKey="Wahome, Newton" sort="Wahome, Newton" uniqKey="Wahome N" first="Newton" last="Wahome">Newton Wahome</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</nlm:affiliation></affiliation></author><author><name sortKey="Mantis, Nicholas J" sort="Mantis, Nicholas J" uniqKey="Mantis N" first="Nicholas J" last="Mantis">Nicholas J. Mantis</name><affiliation><nlm:affiliation>Division of Infectious Disease, Wadsworth Center, New York State Department of Health, Albany, New York 12208.</nlm:affiliation></affiliation></author><author><name sortKey="Middaugh, C Russell" sort="Middaugh, C Russell" uniqKey="Middaugh C" first="C Russell" last="Middaugh">C Russell Middaugh</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047. Electronic address: middaugh@ku.edu.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29763607</idno><idno type="pmid">29763607</idno><idno type="doi">10.1016/j.xphs.2018.05.002</idno><idno type="wicri:Area/PubMed/Corpus">000903</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000903</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Biomedical Applications of Lumazine Synthase.</title><author><name sortKey="Wei, Yangjie" sort="Wei, Yangjie" uniqKey="Wei Y" first="Yangjie" last="Wei">Yangjie Wei</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</nlm:affiliation></affiliation></author><author><name sortKey="Kumar, Prashant" sort="Kumar, Prashant" uniqKey="Kumar P" first="Prashant" last="Kumar">Prashant Kumar</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</nlm:affiliation></affiliation></author><author><name sortKey="Wahome, Newton" sort="Wahome, Newton" uniqKey="Wahome N" first="Newton" last="Wahome">Newton Wahome</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</nlm:affiliation></affiliation></author><author><name sortKey="Mantis, Nicholas J" sort="Mantis, Nicholas J" uniqKey="Mantis N" first="Nicholas J" last="Mantis">Nicholas J. Mantis</name><affiliation><nlm:affiliation>Division of Infectious Disease, Wadsworth Center, New York State Department of Health, Albany, New York 12208.</nlm:affiliation></affiliation></author><author><name sortKey="Middaugh, C Russell" sort="Middaugh, C Russell" uniqKey="Middaugh C" first="C Russell" last="Middaugh">C Russell Middaugh</name><affiliation><nlm:affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047. Electronic address: middaugh@ku.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of pharmaceutical sciences</title><idno type="eISSN">1520-6017</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Drug Delivery Systems (methods)</term><term>Drug Delivery Systems (trends)</term><term>Humans</term><term>Immunogenicity, Vaccine (immunology)</term><term>Multienzyme Complexes (administration & dosage)</term><term>Multienzyme Complexes (chemistry)</term><term>Multienzyme Complexes (immunology)</term><term>Protein Structure, Secondary</term><term>Riboflavin Synthase (administration & dosage)</term><term>Riboflavin Synthase (chemistry)</term><term>Riboflavin Synthase (immunology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="administration & dosage" xml:lang="en"><term>Multienzyme Complexes</term><term>Riboflavin Synthase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Multienzyme Complexes</term><term>Riboflavin Synthase</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Immunogenicity, Vaccine</term><term>Multienzyme Complexes</term><term>Riboflavin Synthase</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Delivery Systems</term></keywords><keywords scheme="MESH" qualifier="trends" xml:lang="en"><term>Drug Delivery Systems</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Humans</term><term>Protein Structure, Secondary</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Lumazine synthase (LS) is a family of enzyme involved in the penultimate step in the biosynthesis of riboflavin. Its enzymatic mechanism has been well defined, and many LS structures have been solved using X-ray crystallography or cryoelectron microscopy. LS is composed of homooligomers, which vary in size and subunit number, including pentamers, decamers, and icosahedral sixty-mers, depending on its species of origin. Research on LS has expanded beyond the initial focus on its enzymatic function to properties related to its oligomeric structure and exceptional conformational stability. These attributes of LS systems have now been repurposed for use in various biomedical fields. This review primarily focuses on the applications of LS as a flexible vaccine presentation system. Presentation of antigens on the surface of LS results in a high local concentration of antigens displayed in an ordered array. Such repetitive structures enable the cross-linking of B-cell receptors and result in strong immune responses through an avidity effect. Potential issues with the use of this system and corresponding solutions are also discussed with the objective of improved utilization of the LS system in vaccine development.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29763607</PMID><DateCompleted><Year>2019</Year><Month>06</Month><Day>07</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-6017</ISSN><JournalIssue CitedMedium="Internet"><Volume>107</Volume><Issue>9</Issue><PubDate><Year>2018</Year><Month>09</Month></PubDate></JournalIssue><Title>Journal of pharmaceutical sciences</Title><ISOAbbreviation>J Pharm Sci</ISOAbbreviation></Journal><ArticleTitle>Biomedical Applications of Lumazine Synthase.</ArticleTitle><Pagination><MedlinePgn>2283-2296</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0022-3549(18)30306-X</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.xphs.2018.05.002</ELocationID><Abstract><AbstractText>Lumazine synthase (LS) is a family of enzyme involved in the penultimate step in the biosynthesis of riboflavin. Its enzymatic mechanism has been well defined, and many LS structures have been solved using X-ray crystallography or cryoelectron microscopy. LS is composed of homooligomers, which vary in size and subunit number, including pentamers, decamers, and icosahedral sixty-mers, depending on its species of origin. Research on LS has expanded beyond the initial focus on its enzymatic function to properties related to its oligomeric structure and exceptional conformational stability. These attributes of LS systems have now been repurposed for use in various biomedical fields. This review primarily focuses on the applications of LS as a flexible vaccine presentation system. Presentation of antigens on the surface of LS results in a high local concentration of antigens displayed in an ordered array. Such repetitive structures enable the cross-linking of B-cell receptors and result in strong immune responses through an avidity effect. Potential issues with the use of this system and corresponding solutions are also discussed with the objective of improved utilization of the LS system in vaccine development.</AbstractText><CopyrightInformation>Copyright © 2018 American Pharmacists Association®. Published by Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wei</LastName><ForeName>Yangjie</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kumar</LastName><ForeName>Prashant</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wahome</LastName><ForeName>Newton</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mantis</LastName><ForeName>Nicholas J</ForeName><Initials>NJ</Initials><AffiliationInfo><Affiliation>Division of Infectious Disease, Wadsworth Center, New York State Department of Health, Albany, New York 12208.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Middaugh</LastName><ForeName>C Russell</ForeName><Initials>CR</Initials><AffiliationInfo><Affiliation>Department of Pharmaceutical Chemistry, Macromolecule and Vaccine Stabilization Center, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047; Department of Pharmaceutical Chemistry, University of Kansas, 2030 Becker Drive, Lawrence, Kansas 66047. Electronic address: middaugh@ku.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>12</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Pharm Sci</MedlineTA><NlmUniqueID>2985195R</NlmUniqueID><ISSNLinking>0022-3549</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009097">Multienzyme Complexes</NameOfSubstance></Chemical><Chemical><RegistryNumber>89287-46-7</RegistryNumber><NameOfSubstance UI="C044822">6,7-dimethyl-8-ribityllumazine synthase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.9</RegistryNumber><NameOfSubstance UI="D012258">Riboflavin Synthase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D016503" MajorTopicYN="N">Drug Delivery Systems</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="N">methods</QualifierName><QualifierName UI="Q000639" MajorTopicYN="Y">trends</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000071497" MajorTopicYN="N">Immunogenicity, Vaccine</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009097" MajorTopicYN="N">Multienzyme Complexes</DescriptorName><QualifierName UI="Q000008" MajorTopicYN="Y">administration & dosage</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012258" MajorTopicYN="N">Riboflavin Synthase</DescriptorName><QualifierName UI="Q000008" MajorTopicYN="Y">administration & dosage</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">adjuvant</Keyword><Keyword MajorTopicYN="Y">drug delivery</Keyword><Keyword MajorTopicYN="Y">immunogenicity</Keyword><Keyword MajorTopicYN="Y">lumazine synthase</Keyword><Keyword MajorTopicYN="Y">polyvalent antigen display</Keyword><Keyword MajorTopicYN="Y">stability</Keyword><Keyword MajorTopicYN="Y">vaccine</Keyword><Keyword MajorTopicYN="Y">virus-like particle</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2018</Year><Month>04</Month><Day>03</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2018</Year><Month>05</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2018</Year><Month>05</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2019</Year><Month>6</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29763607</ArticleId><ArticleId IdType="pii">S0022-3549(18)30306-X</ArticleId><ArticleId IdType="doi">10.1016/j.xphs.2018.05.002</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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