2.50
Hdl Handle:
http://hdl.handle.net/10033/326070
Title:
Antigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers.
Authors:
Arnold, Philipp; Himmels, Patricia; Weiß, Svenja; Decker, Tim-Michael; Markl, Jürgen; Gatterdam, Volker; Tampé, Robert; Bartholomäus, Patrick; Dietrich, Ursula; Dürr, Ralf
Abstract:
HIV-1 is decorated with trimeric glycoprotein spikes that enable infection by engaging CD4 and a chemokine coreceptor, either CCR5 or CXCR4. The variable loop 3 (V3) of the HIV-1 envelope protein (Env) is the main determinant for coreceptor usage. The predominant CCR5 using (R5) HIV-1 Env has been intensively studied in function and structure, whereas the trimeric architecture of the less frequent, but more cytopathic CXCR4 using (X4) HIV-1 Env is largely unknown, as are the consequences of sequence changes in and near V3 on antigenicity and trimeric Env structure.
Citation:
Antigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers. 2014, 11:42 Retrovirology
Journal:
Retrovirology
Issue Date:
2014
URI:
http://hdl.handle.net/10033/326070
DOI:
10.1186/1742-4690-11-42
PubMed ID:
24884925
Type:
Article
Language:
en
ISSN:
1742-4690
Appears in Collections:
publications of the department of experimental infection research ([TC] EXPI)

Full metadata record

DC FieldValue Language
dc.contributor.authorArnold, Philippen
dc.contributor.authorHimmels, Patriciaen
dc.contributor.authorWeiß, Svenjaen
dc.contributor.authorDecker, Tim-Michaelen
dc.contributor.authorMarkl, Jürgenen
dc.contributor.authorGatterdam, Volkeren
dc.contributor.authorTampé, Roberten
dc.contributor.authorBartholomäus, Patricken
dc.contributor.authorDietrich, Ursulaen
dc.contributor.authorDürr, Ralfen
dc.date.accessioned2014-09-12T10:54:52Z-
dc.date.available2014-09-12T10:54:52Z-
dc.date.issued2014-
dc.identifier.citationAntigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers. 2014, 11:42 Retrovirologyen
dc.identifier.issn1742-4690-
dc.identifier.pmid24884925-
dc.identifier.doi10.1186/1742-4690-11-42-
dc.identifier.urihttp://hdl.handle.net/10033/326070-
dc.description.abstractHIV-1 is decorated with trimeric glycoprotein spikes that enable infection by engaging CD4 and a chemokine coreceptor, either CCR5 or CXCR4. The variable loop 3 (V3) of the HIV-1 envelope protein (Env) is the main determinant for coreceptor usage. The predominant CCR5 using (R5) HIV-1 Env has been intensively studied in function and structure, whereas the trimeric architecture of the less frequent, but more cytopathic CXCR4 using (X4) HIV-1 Env is largely unknown, as are the consequences of sequence changes in and near V3 on antigenicity and trimeric Env structure.en
dc.language.isoenen
dc.rightsArchived with thanks to Retrovirologyen
dc.titleAntigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers.en
dc.typeArticleen
dc.identifier.journalRetrovirologyen

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