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Titolo:
Characterization of a macaque recombinant monoclonal antibody that binds to a CD4-induced epitope and neutralizes simian immunodeficiency virus
Autore:
Glamann, J; Hirsch, VM;
Indirizzi:
NIAID Twinbrook II Facil, Mol Microbiol Lab, NIH, Rockville, MD 20852 USA NIAID Twinbrook II Facil Rockville MD USA 20852 , Rockville, MD 20852 USA
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 15, volume: 74, anno: 2000,
pagine: 7158 - 7163
SICI:
0022-538X(200008)74:15<7158:COAMRM>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
PBL-SCID MICE; PASSIVE-IMMUNIZATION; SYNERGISTIC NEUTRALIZATION; ENVELOPE GLYCOPROTEIN; HIV TYPE-1; INFECTION; GP120; SIV; CYNOMOLGUS; RESISTANT;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
44
Recensione:
Indirizzi per estratti:
Indirizzo: Hirsch, VM NIAID Twinbrook II Facil, Mol Microbiol Lab, NIH, 12441 Parklawn Dr, Rockville, MD 20852 USA NIAID Twinbrook II Facil 12441 Parklawn Dr Rockville MD USA 20852
Citazione:
J. Glamann e V.M. Hirsch, "Characterization of a macaque recombinant monoclonal antibody that binds to a CD4-induced epitope and neutralizes simian immunodeficiency virus", J VIROLOGY, 74(15), 2000, pp. 7158-7163

Abstract

A potent neutralizing Fab fragment from a long-term survivor of simian immunodeficiency virus (SIVsm) infection was used to construct a recombinant macaque immunoglobulin G1 kappa (IgG1 kappa) molecule, designated IgG1-201. A Chinese hamster ovary cell line expressing IgG1-201 was derived by stabletransfection and optimized for antibody secretion by methotrexate selection and dihydrofolate reductase gene amplification. IgG1-201 effectively neutralized the homologous, molecularly cloned SIVsmH4 virus but had no activity against the heterologous SIVmac251/BK28 virus. The previously characterized, neutralization-resistant SIVsmE543-3 virus was also not neutralized by IgG1-201. Binding to SIVsmH4 gp120 was enhanced in the presence of recombinant soluble CD4, suggesting that IgG1-201 bound a CD4-induced epitope. IgG1-201 immunoprecipitated the SIVsmH4 but not the SIVsmE543-3 envelope despite a close relationship between these two clones. Immunoprecipitation of a panel of SIVsmH4/SIVsmE543-3 chimeric viruses tentatively assigned the neutralization epitope to the third constant domain, immediately C terminal to the V3 loop. These findings suggest the presence of at least one CD4-inducedneutralization epitope on SIV as is the case with human immunodeficiency virus type 1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 21:50:42