Epitope mapping studies of snake venom phospholipase A2 using monoclonal antibodies.
Identifieur interne : 000498 ( Ncbi/Merge ); précédent : 000497; suivant : 000499Epitope mapping studies of snake venom phospholipase A2 using monoclonal antibodies.
Auteurs : B G Stiles [États-Unis] ; J L MiddlebrookSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 1991.
Descripteurs français
- KwdFr :
- Animaux, Anticorps monoclonaux, Cartographie peptidique, Données de séquences moléculaires, Fixation compétitive, Peptides (), Peptides (immunologie), Phospholipases A (), Phospholipases A (immunologie), Phospholipases A2, Sites de fixation, Séquence d'acides aminés, Venins des élapidés (), Venins des élapidés (immunologie), Épitopes ().
- MESH :
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Antibodies, Monoclonal, Binding Sites, Binding, Competitive, Elapid Venoms (chemistry), Elapid Venoms (immunology), Epitopes (chemistry), Molecular Sequence Data, Peptide Mapping, Peptides (chemistry), Peptides (immunology), Phospholipases A (chemistry), Phospholipases A (immunology), Phospholipases A2.
- MESH :
- chemical , chemistry : Elapid Venoms, Epitopes, Peptides, Phospholipases A.
- chemical , immunology : Elapid Venoms, Peptides, Phospholipases A.
- chemical : Antibodies, Monoclonal, Phospholipases A2.
- Amino Acid Sequence, Animals, Binding Sites, Binding, Competitive, Molecular Sequence Data, Peptide Mapping.
Abstract
Fifteen different monoclonal antibodies developed against pseudexin, a snake venom phospholipase A2 with presynaptic neurotoxicity, were screened for linear epitope recognition. Peptides (9-mers) spanning pseudexin were synthesized by using alanine-derivatized polyethylene pins and subsequently probed with antibody. Four antibodies bound to toxin peptides and were detected with an enzyme-linked immunosorbent assay. Three of the bound antibodies recognized a site important in calcium binding and the interlocking of dimeric forms of snake venom phospholipase A2. Analogous regions from other phospholipases were synthesized and probed with the four reactive antibodies. A good correlation was found between the reactivity of whole molecule phospholipases and peptide regions with the antibodies. Monoclonal antibodies neutralizing the lethal or enzymatic effects of pseudexin did not recognize any linear epitopes.
DOI: 10.1007/978-1-4684-6000-1_27
PubMed: 1725235
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(immunology)</term><term>Epitopes (chemistry)</term><term>Molecular Sequence Data</term><term>Peptide Mapping</term><term>Peptides (chemistry)</term><term>Peptides (immunology)</term><term>Phospholipases A (chemistry)</term><term>Phospholipases A (immunology)</term><term>Phospholipases A2</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Anticorps monoclonaux</term><term>Cartographie peptidique</term><term>Données de séquences moléculaires</term><term>Fixation compétitive</term><term>Peptides ()</term><term>Peptides (immunologie)</term><term>Phospholipases A ()</term><term>Phospholipases A (immunologie)</term><term>Phospholipases A2</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Venins des élapidés ()</term><term>Venins des élapidés (immunologie)</term><term>Épitopes ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Elapid 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compétitive</term><term>Peptides</term><term>Phospholipases A</term><term>Phospholipases A2</term><term>Sites de fixation</term><term>Séquence d'acides aminés</term><term>Venins des élapidés</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Fifteen different monoclonal antibodies developed against pseudexin, a snake venom phospholipase A2 with presynaptic neurotoxicity, were screened for linear epitope recognition. Peptides (9-mers) spanning pseudexin were synthesized by using alanine-derivatized polyethylene pins and subsequently probed with antibody. Four antibodies bound to toxin peptides and were detected with an enzyme-linked immunosorbent assay. Three of the bound antibodies recognized a site important in calcium binding and the interlocking of dimeric forms of snake venom phospholipase A2. Analogous regions from other phospholipases were synthesized and probed with the four reactive antibodies. A good correlation was found between the reactivity of whole molecule phospholipases and peptide regions with the antibodies. Monoclonal antibodies neutralizing the lethal or enzymatic effects of pseudexin did not recognize any linear epitopes.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1725235</PMID><DateCompleted><Year>1992</Year><Month>05</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>22</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0065-2598</ISSN><JournalIssue CitedMedium="Print"><Volume>303</Volume><PubDate><Year>1991</Year></PubDate></JournalIssue><Title>Advances in experimental medicine and biology</Title><ISOAbbreviation>Adv. Exp. Med. Biol.</ISOAbbreviation></Journal><ArticleTitle>Epitope mapping studies of snake venom phospholipase A2 using monoclonal antibodies.</ArticleTitle><Pagination><MedlinePgn>243-8</MedlinePgn></Pagination><Abstract><AbstractText>Fifteen different monoclonal antibodies developed against pseudexin, a snake venom phospholipase A2 with presynaptic neurotoxicity, were screened for linear epitope recognition. Peptides (9-mers) spanning pseudexin were synthesized by using alanine-derivatized polyethylene pins and subsequently probed with antibody. Four antibodies bound to toxin peptides and were detected with an enzyme-linked immunosorbent assay. Three of the bound antibodies recognized a site important in calcium binding and the interlocking of dimeric forms of snake venom phospholipase A2. Analogous regions from other phospholipases were synthesized and probed with the four reactive antibodies. A good correlation was found between the reactivity of whole molecule phospholipases and peptide regions with the antibodies. Monoclonal antibodies neutralizing the lethal or enzymatic effects of pseudexin did not recognize any linear epitopes.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stiles</LastName><ForeName>B G</ForeName><Initials>BG</Initials><AffiliationInfo><Affiliation>Department of Toxicology, U.S. Army Medical Research Institute of Infectious Diseases, Frederick, Maryland 21702-50112.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Middlebrook</LastName><ForeName>J L</ForeName><Initials>JL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Adv Exp Med Biol</MedlineTA><NlmUniqueID>0121103</NlmUniqueID><ISSNLinking>0065-2598</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000911">Antibodies, Monoclonal</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004546">Elapid Venoms</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C026235">Pseudechis venom</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.32</RegistryNumber><NameOfSubstance UI="D010741">Phospholipases A</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.1.4</RegistryNumber><NameOfSubstance UI="D054467">Phospholipases A2</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000911" MajorTopicYN="N">Antibodies, Monoclonal</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001667" MajorTopicYN="N">Binding, Competitive</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004546" MajorTopicYN="N">Elapid Venoms</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010449" MajorTopicYN="N">Peptide Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010741" MajorTopicYN="N">Phospholipases A</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054467" MajorTopicYN="N">Phospholipases A2</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>1</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>1</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1725235</ArticleId><ArticleId IdType="doi">10.1007/978-1-4684-6000-1_27</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region></list><tree><noCountry><name sortKey="Middlebrook, J L" sort="Middlebrook, J L" uniqKey="Middlebrook J" first="J L" last="Middlebrook">J L Middlebrook</name></noCountry><country name="États-Unis"><region name="Maryland"><name sortKey="Stiles, B G" sort="Stiles, B G" uniqKey="Stiles B" first="B G" last="Stiles">B G Stiles</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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