Hemolymph protease-5 links the melanization and Toll immune pathways in the tobacco hornworm, Manduca sexta.
Identifieur interne : 000142 ( Main/Exploration ); précédent : 000141; suivant : 000143Hemolymph protease-5 links the melanization and Toll immune pathways in the tobacco hornworm, Manduca sexta.
Auteurs : Yang Wang [États-Unis] ; Fan Yang [États-Unis] ; Xiaolong Cao [États-Unis] ; Zhen Zou [États-Unis] ; Zhiqiang Lu [États-Unis] ; Michael R. Kanost [États-Unis] ; Haobo Jiang [États-Unis]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2020.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Hémolymphe (enzymologie), Hémolymphe (immunologie), Manduca (enzymologie), Manduca (immunologie), Manduca (métabolisme), Protéases à sérine (immunologie), Protéases à sérine (métabolisme), Protéines d'insecte (immunologie), Protéines d'insecte (métabolisme), Récepteurs de type Toll (immunologie), Récepteurs de type Toll (métabolisme), Transduction du signal (MeSH).
- MESH :
- enzymologie : Hémolymphe, Manduca.
- immunologie : Hémolymphe, Manduca, Protéases à sérine, Protéines d'insecte, Récepteurs de type Toll.
- métabolisme : Manduca, Protéases à sérine, Protéines d'insecte, Récepteurs de type Toll.
- Animaux, Transduction du signal.
English descriptors
- KwdEn :
- Animals (MeSH), Hemolymph (enzymology), Hemolymph (immunology), Insect Proteins (immunology), Insect Proteins (metabolism), Manduca (enzymology), Manduca (immunology), Manduca (metabolism), Serine Proteases (immunology), Serine Proteases (metabolism), Signal Transduction (MeSH), Toll-Like Receptors (immunology), Toll-Like Receptors (metabolism).
- MESH :
- chemical , immunology : Insect Proteins, Serine Proteases, Toll-Like Receptors.
- enzymology : Hemolymph, Manduca.
- immunology : Hemolymph, Manduca.
- chemical , metabolism : Insect Proteins, Manduca, Serine Proteases, Toll-Like Receptors.
- Animals, Signal Transduction.
Abstract
Proteolytic activation of phenoloxidase (PO) and the cytokine Spätzle during immune responses of insects is mediated by a network of hemolymph serine proteases (HPs) and noncatalytic serine protease homologs (SPHs) and inhibited by serpins. However, integration and conservation of the system and its control mechanisms are not fully understood. Here we present biochemical evidence that PO-catalyzed melanin formation, Spätzle-triggered Toll activation, and induced synthesis of antimicrobial peptides are stimulated via hemolymph (serine) protease 5 (HP5) in Manduca sexta Previous studies have demonstrated a protease cascade pathway in which HP14 activates proHP21; HP21 activates proPAP2 and proPAP3, which then activate proPO in the presence of a complex of SPH1 and SPH2. We found that both HP21 and PAP3 activate proHP5 by cleavage at ESDR176*IIGG. HP5 then cleaves proHP6 at a unique site of LDLH112*ILGG. HP6, an ortholog of Drosophila Persephone, activates both proHP8 and proPAP1. HP8 activates proSpätzle-1, whereas PAP1 cleaves and activates proPO. HP5 is inhibited by Manduca sexta serpin-4, serpin-1A, and serpin-1J to regulate its activity. In summary, we have elucidated the physiological roles of HP5, a CLIPB with unique cleavage specificity (cutting after His) that coordinates immune responses in the caterpillar.
DOI: 10.1073/pnas.2004761117
PubMed: 32900946
PubMed Central: PMC7519321
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Kanost</name><affiliation wicri:level="2"><nlm:affiliation>Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Kansas</region></placeName><wicri:cityArea>Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan</wicri:cityArea></affiliation></author><author><name sortKey="Jiang, Haobo" sort="Jiang, Haobo" uniqKey="Jiang H" first="Haobo" last="Jiang">Haobo Jiang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078; haobo.jiang@okstate.edu.</nlm:affiliation><country wicri:rule="url">États-Unis</country><wicri:regionArea>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater</wicri:regionArea><wicri:noRegion>Stillwater</wicri:noRegion></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="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Hemolymph (enzymology)</term><term>Hemolymph (immunology)</term><term>Insect Proteins (immunology)</term><term>Insect Proteins (metabolism)</term><term>Manduca (enzymology)</term><term>Manduca (immunology)</term><term>Manduca (metabolism)</term><term>Serine Proteases (immunology)</term><term>Serine Proteases (metabolism)</term><term>Signal Transduction (MeSH)</term><term>Toll-Like Receptors (immunology)</term><term>Toll-Like Receptors (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Hémolymphe (enzymologie)</term><term>Hémolymphe (immunologie)</term><term>Manduca (enzymologie)</term><term>Manduca (immunologie)</term><term>Manduca (métabolisme)</term><term>Protéases à sérine (immunologie)</term><term>Protéases à sérine (métabolisme)</term><term>Protéines d'insecte (immunologie)</term><term>Protéines d'insecte (métabolisme)</term><term>Récepteurs de type Toll (immunologie)</term><term>Récepteurs de type Toll (métabolisme)</term><term>Transduction du signal (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Insect Proteins</term><term>Serine Proteases</term><term>Toll-Like Receptors</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Hémolymphe</term><term>Manduca</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Hemolymph</term><term>Manduca</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Hémolymphe</term><term>Manduca</term><term>Protéases à sérine</term><term>Protéines d'insecte</term><term>Récepteurs de type Toll</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Hemolymph</term><term>Manduca</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Insect Proteins</term><term>Manduca</term><term>Serine Proteases</term><term>Toll-Like Receptors</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Manduca</term><term>Protéases à sérine</term><term>Protéines d'insecte</term><term>Récepteurs de type Toll</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Proteolytic activation of phenoloxidase (PO) and the cytokine Spätzle during immune responses of insects is mediated by a network of hemolymph serine proteases (HPs) and noncatalytic serine protease homologs (SPHs) and inhibited by serpins. However, integration and conservation of the system and its control mechanisms are not fully understood. Here we present biochemical evidence that PO-catalyzed melanin formation, Spätzle-triggered Toll activation, and induced synthesis of antimicrobial peptides are stimulated via hemolymph (serine) protease 5 (HP5) in <i>Manduca sexta</i> Previous studies have demonstrated a protease cascade pathway in which HP14 activates proHP21; HP21 activates proPAP2 and proPAP3, which then activate proPO in the presence of a complex of SPH1 and SPH2. We found that both HP21 and PAP3 activate proHP5 by cleavage at ESDR<sup>176</sup>*IIGG. HP5 then cleaves proHP6 at a unique site of LDLH<sup>112</sup>*ILGG. HP6, an ortholog of <i>Drosophila</i> Persephone, activates both proHP8 and proPAP1. HP8 activates proSpätzle-1, whereas PAP1 cleaves and activates proPO. HP5 is inhibited by <i>Manduca sexta</i> serpin-4, serpin-1A, and serpin-1J to regulate its activity. In summary, we have elucidated the physiological roles of HP5, a CLIPB with unique cleavage specificity (cutting after His) that coordinates immune responses in the caterpillar.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32900946</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>17</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>17</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>117</Volume><Issue>38</Issue><PubDate><Year>2020</Year><Month>09</Month><Day>22</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>Hemolymph protease-5 links the melanization and Toll immune pathways in the tobacco hornworm, <i>Manduca sexta</i>.</ArticleTitle><Pagination><MedlinePgn>23581-23587</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.2004761117</ELocationID><Abstract><AbstractText>Proteolytic activation of phenoloxidase (PO) and the cytokine Spätzle during immune responses of insects is mediated by a network of hemolymph serine proteases (HPs) and noncatalytic serine protease homologs (SPHs) and inhibited by serpins. However, integration and conservation of the system and its control mechanisms are not fully understood. Here we present biochemical evidence that PO-catalyzed melanin formation, Spätzle-triggered Toll activation, and induced synthesis of antimicrobial peptides are stimulated via hemolymph (serine) protease 5 (HP5) in <i>Manduca sexta</i> Previous studies have demonstrated a protease cascade pathway in which HP14 activates proHP21; HP21 activates proPAP2 and proPAP3, which then activate proPO in the presence of a complex of SPH1 and SPH2. We found that both HP21 and PAP3 activate proHP5 by cleavage at ESDR<sup>176</sup>*IIGG. HP5 then cleaves proHP6 at a unique site of LDLH<sup>112</sup>*ILGG. HP6, an ortholog of <i>Drosophila</i> Persephone, activates both proHP8 and proPAP1. HP8 activates proSpätzle-1, whereas PAP1 cleaves and activates proPO. HP5 is inhibited by <i>Manduca sexta</i> serpin-4, serpin-1A, and serpin-1J to regulate its activity. In summary, we have elucidated the physiological roles of HP5, a CLIPB with unique cleavage specificity (cutting after His) that coordinates immune responses in the caterpillar.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yang</ForeName><Initials>Y</Initials><Identifier Source="ORCID">0000-0002-1202-9965</Identifier><AffiliationInfo><Affiliation>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Fan</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cao</LastName><ForeName>Xiaolong</ForeName><Initials>X</Initials><Identifier Source="ORCID">0000-0001-8124-7491</Identifier><AffiliationInfo><Affiliation>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Zou</LastName><ForeName>Zhen</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lu</LastName><ForeName>Zhiqiang</ForeName><Initials>Z</Initials><AffiliationInfo><Affiliation>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kanost</LastName><ForeName>Michael R</ForeName><Initials>MR</Initials><AffiliationInfo><Affiliation>Department of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS 66506.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jiang</LastName><ForeName>Haobo</ForeName><Initials>H</Initials><Identifier Source="ORCID">0000-0003-1357-1315</Identifier><AffiliationInfo><Affiliation>Department of Entomology and Plant Pathology, Oklahoma State University, Stillwater, OK 74078; haobo.jiang@okstate.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM058634</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R21 AI139998</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>09</Month><Day>08</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="D019476">Insect Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D051193">Toll-Like Receptors</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.-</RegistryNumber><NameOfSubstance UI="D057057">Serine Proteases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006458" MajorTopicYN="Y">Hemolymph</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D019476" MajorTopicYN="Y">Insect Proteins</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018402" MajorTopicYN="Y">Manduca</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057057" MajorTopicYN="Y">Serine Proteases</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051193" MajorTopicYN="N">Toll-Like Receptors</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">clip domain</Keyword><Keyword MajorTopicYN="Y">hemolymph protein</Keyword><Keyword MajorTopicYN="Y">insect immunity</Keyword><Keyword MajorTopicYN="Y">serine protease cascade</Keyword><Keyword MajorTopicYN="Y">zymogen activation</Keyword></KeywordList><CoiStatement>The authors declare no competing interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pmc-release"><Year>2021</Year><Month>03</Month><Day>08</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>9</Month><Day>10</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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IdType="pubmed">19900472</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Kansas</li><li>Oklahoma</li></region></list><tree><country name="États-Unis"><region name="Oklahoma"><name sortKey="Wang, Yang" sort="Wang, Yang" uniqKey="Wang Y" first="Yang" last="Wang">Yang Wang</name></region><name sortKey="Cao, Xiaolong" sort="Cao, Xiaolong" uniqKey="Cao X" first="Xiaolong" last="Cao">Xiaolong Cao</name><name sortKey="Jiang, Haobo" sort="Jiang, Haobo" uniqKey="Jiang H" first="Haobo" last="Jiang">Haobo Jiang</name><name sortKey="Kanost, Michael R" sort="Kanost, Michael R" uniqKey="Kanost M" first="Michael R" last="Kanost">Michael R. Kanost</name><name sortKey="Lu, Zhiqiang" sort="Lu, Zhiqiang" uniqKey="Lu Z" first="Zhiqiang" last="Lu">Zhiqiang Lu</name><name sortKey="Yang, Fan" sort="Yang, Fan" uniqKey="Yang F" first="Fan" last="Yang">Fan Yang</name><name sortKey="Zou, Zhen" sort="Zou, Zhen" uniqKey="Zou Z" first="Zhen" last="Zou">Zhen Zou</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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