Article: Identification of a novel CD4i human monoclonal antibody Fab that neutralizes HIV-1 primary isolates from different clades

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TitleIdentification of a novel CD4i human monoclonal antibody Fab that neutralizes HIV-1 primary isolates from different clades
AuthorsZhang, MY1 2
Shu, Y2
Sidorov, I2
Dimitrov, DS2
Issue Date2004
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/antiviral
CitationAntiviral Research, 2004, v. 61 n. 3, p. 161-164 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.antiviral.2003.09.009
AbstractA new human monoclonal antibody (hmAb), designated m16, was selected by sequential antigen panning (SAP) of a human phage display library against recombinant soluble HIV-1 envelope glycoproteins (Envs) (gp140s) and their complexes with soluble CD4. It bound with high (nM) affinity to gp120 and gp140; the binding was further enhanced by interactions of the Envs with CD4. m16 inhibited cell fusion mediated by the Envs of 9 HIV-1 isolates from clades A, B, E and G with potency on average comparable to that of the broadly neutralizing human monoclonal antibody Fab X5. The identification of a new hmAb with broad neutralizing activity that exhibits differential inhibitory profile suggests a potential for its use as a component of anti-HIV-1 treatments.
ISSN0166-3542
2011 Impact Factor: 4.301
2011 SCImago Journal Rankings: 0.393
DOIhttp://dx.doi.org/10.1016/j.antiviral.2003.09.009
ReferencesReferences in Scopus
DC Field
Value
dc.contributor.authorZhang, MY
dc.contributor.authorShu, Y
dc.contributor.authorSidorov, I
dc.contributor.authorDimitrov, DS
dc.date.accessioned2012-08-08T08:49:29Z
dc.date.available2012-08-08T08:49:29Z
dc.date.issued2004
dc.description.abstractA new human monoclonal antibody (hmAb), designated m16, was selected by sequential antigen panning (SAP) of a human phage display library against recombinant soluble HIV-1 envelope glycoproteins (Envs) (gp140s) and their complexes with soluble CD4. It bound with high (nM) affinity to gp120 and gp140; the binding was further enhanced by interactions of the Envs with CD4. m16 inhibited cell fusion mediated by the Envs of 9 HIV-1 isolates from clades A, B, E and G with potency on average comparable to that of the broadly neutralizing human monoclonal antibody Fab X5. The identification of a new hmAb with broad neutralizing activity that exhibits differential inhibitory profile suggests a potential for its use as a component of anti-HIV-1 treatments.
dc.description.natureLink_to_subscribed_fulltext
dc.identifier.citationAntiviral Research, 2004, v. 61 n. 3, p. 161-164 [How to Cite?]
DOI: http://dx.doi.org/10.1016/j.antiviral.2003.09.009
dc.identifier.doihttp://dx.doi.org/10.1016/j.antiviral.2003.09.009
dc.identifier.epage164
dc.identifier.isiWOS:000189131000003
dc.identifier.issn0166-3542
2011 Impact Factor: 4.301
2011 SCImago Journal Rankings: 0.393
dc.identifier.issue3
dc.identifier.pmid15168796
dc.identifier.scopuseid_2-s2.0-0842311270
dc.identifier.spage161
dc.identifier.urihttp://hdl.handle.net/10722/157381
dc.identifier.volume61
dc.languageeng
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/antiviral
dc.publisher.placeNetherlands
dc.relation.ispartofAntiviral Research
dc.relation.referencesReferences in Scopus
dc.subject.meshAntibodies, Monoclonal - Immunology
dc.subject.meshAntibody Affinity
dc.subject.meshAntigens, Cd4 - Immunology
dc.subject.meshCell Fusion
dc.subject.meshGene Products, Env - Immunology
dc.subject.meshGenotype
dc.subject.meshHiv Antibodies - Immunology
dc.subject.meshHiv Antigens - Immunology
dc.subject.meshHiv Envelope Protein Gp120 - Immunology
dc.subject.meshHiv-1 - Genetics - Immunology
dc.subject.meshHumans
dc.subject.meshImmunoglobulin Fab Fragments - Immunology
dc.subject.meshNeutralization Tests
dc.subject.meshPeptide Library
dc.subject.meshProtein Binding
dc.subject.meshRecombinant Proteins - Immunology
dc.subject.meshEnv Gene Products, Human Immunodeficiency Virus
dc.titleIdentification of a novel CD4i human monoclonal antibody Fab that neutralizes HIV-1 primary isolates from different clades
dc.typeArticle
Author Affiliations
  1. SAIC-Frederick
  2. National Institutes of Health, Bethesda