A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: individual patterns of reactivity in human sera.
Identifieur interne : 002995 ( PubMed/Curation ); précédent : 002994; suivant : 002996A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: individual patterns of reactivity in human sera.
Auteurs : P J Klasse [Suède] ; R. Pipkorn ; J. BlombergSource :
- Molecular immunology [ 0161-5890 ] ; 1991.
Descripteurs français
- KwdFr :
- Conformation moléculaire, Données de séquences moléculaires, Humains, Protéine d'enveloppe gp41 du VIH (immunologie), Sites de fixation des anticorps, Séquence d'acides aminés, Techniques immunoenzymatiques, Techniques in vitro, Thréonine (immunologie), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (immunologie), Épitopes.
- MESH :
- immunologie : Protéine d'enveloppe gp41 du VIH, Thréonine, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- Conformation moléculaire, Données de séquences moléculaires, Humains, Sites de fixation des anticorps, Séquence d'acides aminés, Techniques immunoenzymatiques, Techniques in vitro, Épitopes.
English descriptors
- KwdEn :
- MESH :
- chemical , immunology : HIV Envelope Protein gp41, Threonine.
- chemical : Epitopes.
- immunology : HIV-1.
- Amino Acid Sequence, Binding Sites, Antibody, Humans, Immunoenzyme Techniques, In Vitro Techniques, Molecular Conformation, Molecular Sequence Data.
Abstract
We investigated the antigenicity of a highly conserved region in the transmembrane protein of the human immunodeficiency virus type 1 (HIV-1). In order to identify antigenically important residues, amino-acid sequences of synthetic peptides representing this region were varied systematically: single residues were omitted from the sequence of HIV-env 583-599; threonines were substituted for pairs of residues in HIV-env 581-599; the sequences of heptadeca-peptides were shifted by single residues. The peptides were tested in an enzyme immuno-assay against fourteen HIV-1 antibody-positive human sera, which were previously found to react with HIV-env 583-599, and against rabbit antisera to the peptides HIV-env 583-599 and 586-606. Substitutions as well as deletions in the sequence 589-596 (AVERYLKD) aborgated the antigenicity of the peptides with most of the human sera. Changes outside this sequence affected the reactivities differentially. Six overlapping dodeca-peptides, shifted in the sequence by single residues, lacked antigenicity in a competition assay, suggesting antigenic dependence on an ordered peptide conformation, which the longer peptides may preferentially assume. 19- and 21-mers with overlapping sequences competed to different extents with each other for binding to the antibodies of 3 human sera, illustrating that more than one antigenic structure in this narrow region can be recognized by a single polyclonal serum.
DOI: 10.1016/0161-5890(91)90130-c
PubMed: 1713646
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :002995
Links to Exploration step
pubmed:1713646Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: individual patterns of reactivity in human sera.</title><author><name sortKey="Klasse, P J" sort="Klasse, P J" uniqKey="Klasse P" first="P J" last="Klasse">P J Klasse</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medical Microbiology, University of Lund, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Microbiology, University of Lund</wicri:regionArea></affiliation></author><author><name sortKey="Pipkorn, R" sort="Pipkorn, R" uniqKey="Pipkorn R" first="R" last="Pipkorn">R. Pipkorn</name></author><author><name sortKey="Blomberg, J" sort="Blomberg, J" uniqKey="Blomberg J" first="J" last="Blomberg">J. Blomberg</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1713646</idno><idno type="pmid">1713646</idno><idno type="doi">10.1016/0161-5890(91)90130-c</idno><idno type="wicri:Area/PubMed/Corpus">002995</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">002995</idno><idno type="wicri:Area/PubMed/Curation">002995</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">002995</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: individual patterns of reactivity in human sera.</title><author><name sortKey="Klasse, P J" sort="Klasse, P J" uniqKey="Klasse P" first="P J" last="Klasse">P J Klasse</name><affiliation wicri:level="1"><nlm:affiliation>Department of Medical Microbiology, University of Lund, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Medical Microbiology, University of Lund</wicri:regionArea></affiliation></author><author><name sortKey="Pipkorn, R" sort="Pipkorn, R" uniqKey="Pipkorn R" first="R" last="Pipkorn">R. Pipkorn</name></author><author><name sortKey="Blomberg, J" sort="Blomberg, J" uniqKey="Blomberg J" first="J" last="Blomberg">J. Blomberg</name></author></analytic><series><title level="j">Molecular immunology</title><idno type="ISSN">0161-5890</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites, Antibody</term><term>Epitopes</term><term>HIV Envelope Protein gp41 (immunology)</term><term>HIV-1 (immunology)</term><term>Humans</term><term>Immunoenzyme Techniques</term><term>In Vitro Techniques</term><term>Molecular Conformation</term><term>Molecular Sequence Data</term><term>Threonine (immunology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Conformation moléculaire</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Protéine d'enveloppe gp41 du VIH (immunologie)</term><term>Sites de fixation des anticorps</term><term>Séquence d'acides aminés</term><term>Techniques immunoenzymatiques</term><term>Techniques in vitro</term><term>Thréonine (immunologie)</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (immunologie)</term><term>Épitopes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>HIV Envelope Protein gp41</term><term>Threonine</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Epitopes</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Protéine d'enveloppe gp41 du VIH</term><term>Thréonine</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>HIV-1</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Binding Sites, Antibody</term><term>Humans</term><term>Immunoenzyme Techniques</term><term>In Vitro Techniques</term><term>Molecular Conformation</term><term>Molecular Sequence Data</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Conformation moléculaire</term><term>Données de séquences moléculaires</term><term>Humains</term><term>Sites de fixation des anticorps</term><term>Séquence d'acides aminés</term><term>Techniques immunoenzymatiques</term><term>Techniques in vitro</term><term>Épitopes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We investigated the antigenicity of a highly conserved region in the transmembrane protein of the human immunodeficiency virus type 1 (HIV-1). In order to identify antigenically important residues, amino-acid sequences of synthetic peptides representing this region were varied systematically: single residues were omitted from the sequence of HIV-env 583-599; threonines were substituted for pairs of residues in HIV-env 581-599; the sequences of heptadeca-peptides were shifted by single residues. The peptides were tested in an enzyme immuno-assay against fourteen HIV-1 antibody-positive human sera, which were previously found to react with HIV-env 583-599, and against rabbit antisera to the peptides HIV-env 583-599 and 586-606. Substitutions as well as deletions in the sequence 589-596 (AVERYLKD) aborgated the antigenicity of the peptides with most of the human sera. Changes outside this sequence affected the reactivities differentially. Six overlapping dodeca-peptides, shifted in the sequence by single residues, lacked antigenicity in a competition assay, suggesting antigenic dependence on an ordered peptide conformation, which the longer peptides may preferentially assume. 19- and 21-mers with overlapping sequences competed to different extents with each other for binding to the antibodies of 3 human sera, illustrating that more than one antigenic structure in this narrow region can be recognized by a single polyclonal serum.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1713646</PMID><DateCompleted><Year>1991</Year><Month>09</Month><Day>03</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>24</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0161-5890</ISSN><JournalIssue CitedMedium="Print"><Volume>28</Volume><Issue>6</Issue><PubDate><Year>1991</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Molecular immunology</Title><ISOAbbreviation>Mol. Immunol.</ISOAbbreviation></Journal><ArticleTitle>A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: individual patterns of reactivity in human sera.</ArticleTitle><Pagination><MedlinePgn>613-22</MedlinePgn></Pagination><Abstract><AbstractText>We investigated the antigenicity of a highly conserved region in the transmembrane protein of the human immunodeficiency virus type 1 (HIV-1). In order to identify antigenically important residues, amino-acid sequences of synthetic peptides representing this region were varied systematically: single residues were omitted from the sequence of HIV-env 583-599; threonines were substituted for pairs of residues in HIV-env 581-599; the sequences of heptadeca-peptides were shifted by single residues. The peptides were tested in an enzyme immuno-assay against fourteen HIV-1 antibody-positive human sera, which were previously found to react with HIV-env 583-599, and against rabbit antisera to the peptides HIV-env 583-599 and 586-606. Substitutions as well as deletions in the sequence 589-596 (AVERYLKD) aborgated the antigenicity of the peptides with most of the human sera. Changes outside this sequence affected the reactivities differentially. Six overlapping dodeca-peptides, shifted in the sequence by single residues, lacked antigenicity in a competition assay, suggesting antigenic dependence on an ordered peptide conformation, which the longer peptides may preferentially assume. 19- and 21-mers with overlapping sequences competed to different extents with each other for binding to the antibodies of 3 human sera, illustrating that more than one antigenic structure in this narrow region can be recognized by a single polyclonal serum.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Klasse</LastName><ForeName>P J</ForeName><Initials>PJ</Initials><AffiliationInfo><Affiliation>Department of Medical Microbiology, University of Lund, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pipkorn</LastName><ForeName>R</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Blomberg</LastName><ForeName>J</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Mol Immunol</MedlineTA><NlmUniqueID>7905289</NlmUniqueID><ISSNLinking>0161-5890</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000939">Epitopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015700">HIV Envelope Protein gp41</NameOfSubstance></Chemical><Chemical><RegistryNumber>2ZD004190S</RegistryNumber><NameOfSubstance UI="D013912">Threonine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CitationSubset>X</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001666" MajorTopicYN="N">Binding Sites, Antibody</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000939" MajorTopicYN="N">Epitopes</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015700" MajorTopicYN="N">HIV Envelope Protein gp41</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015497" MajorTopicYN="N">HIV-1</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007124" MajorTopicYN="N">Immunoenzyme Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D066298" MajorTopicYN="N">In Vitro Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008968" MajorTopicYN="N">Molecular Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013912" MajorTopicYN="N">Threonine</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>6</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>6</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>6</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1713646</ArticleId><ArticleId IdType="doi">10.1016/0161-5890(91)90130-c</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/PubMed/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002995 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd -nk 002995 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= PubMed
|étape= Curation
|type= RBID
|clé= pubmed:1713646
|texte= A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: individual patterns of reactivity in human sera.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:1713646" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |