Epitope mapping studies of snake venom phospholipase A2 using monoclonal antibodies.
Identifieur interne : 002A11 ( PubMed/Corpus ); précédent : 002A10; suivant : 002A12Epitope mapping studies of snake venom phospholipase A2 using monoclonal antibodies.
Auteurs : B G Stiles ; J L MiddlebrookSource :
- Advances in experimental medicine and biology [ 0065-2598 ] ; 1991.
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
Links to Exploration step
pubmed:1725235Le document en format XML
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<author><name sortKey="Stiles, B G" sort="Stiles, B G" uniqKey="Stiles B" first="B G" last="Stiles">B G Stiles</name>
<affiliation><nlm:affiliation>Department of Toxicology, U.S. Army Medical Research Institute of Infectious Diseases, Frederick, Maryland 21702-50112.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="Middlebrook, J L" sort="Middlebrook, J L" uniqKey="Middlebrook J" first="J L" last="Middlebrook">J L Middlebrook</name>
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<author><name sortKey="Stiles, B G" sort="Stiles, B G" uniqKey="Stiles B" first="B G" last="Stiles">B G Stiles</name>
<affiliation><nlm:affiliation>Department of Toxicology, U.S. Army Medical Research Institute of Infectious Diseases, Frederick, Maryland 21702-50112.</nlm:affiliation>
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<term>Animals</term>
<term>Antibodies, Monoclonal</term>
<term>Binding Sites</term>
<term>Binding, Competitive</term>
<term>Elapid Venoms (chemistry)</term>
<term>Elapid Venoms (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>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Elapid Venoms</term>
<term>Epitopes</term>
<term>Peptides</term>
<term>Phospholipases A</term>
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<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Elapid Venoms</term>
<term>Peptides</term>
<term>Phospholipases A</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Antibodies, Monoclonal</term>
<term>Phospholipases A2</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
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<term>Binding Sites</term>
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<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>
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<Title>Advances in experimental medicine and biology</Title>
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<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>
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<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
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