MOUSE MONOCLONAL-ANTIBODIES TO HUMAN-IMMUNODEFICIENCY-VIRUS GLYCOPROTEIN-120 GENERATED BY REPEATED IMMUNIZATION WITH GLYCOPROTEIN-120 FROM A SINGLE ISOLATE, OR BY SEQUENTIAL IMMUNIZATION WITH GLYCOPROTEIN-120 FROM 3 ISOLATES

Citation
Jp. Reeves et al., MOUSE MONOCLONAL-ANTIBODIES TO HUMAN-IMMUNODEFICIENCY-VIRUS GLYCOPROTEIN-120 GENERATED BY REPEATED IMMUNIZATION WITH GLYCOPROTEIN-120 FROM A SINGLE ISOLATE, OR BY SEQUENTIAL IMMUNIZATION WITH GLYCOPROTEIN-120 FROM 3 ISOLATES, Hybridoma, 14(3), 1995, pp. 235-242
Citations number
22
Categorie Soggetti
Immunology
Journal title
ISSN journal
0272457X
Volume
14
Issue
3
Year of publication
1995
Pages
235 - 242
Database
ISI
SICI code
0272-457X(1995)14:3<235:MMTHG>2.0.ZU;2-P
Abstract
Mouse hybridomas were isolated that produce monoclonal antibodies (MAb s) to several regions of the HIV envelope, gp120, which may be used to map immunogenic regions in animal and human immunity, One series of M Abs was generated by repeated immunization with recombinant gp120 (rgp 120) from a single isolate, and a second series by sequential immuniza tion with rgp120 from three isolates, All MAbs bound to rgp120(IIIB), but only one bound well to cell surface-expressed gp160, Synthetic pep tides spanning much of the length of gp120 were used to map MAb reacti vity, Two MAbs were mapped to the C1 region, one to the C2 region, and three to the C5 region by this approach, Six distinct epitopes were d etected by competitive binding analysis. One MAb binding in the C1 reg ion blocks binding of CD4 to rgp120(IIIB), binds by ELISA to rgp120(MN ) (an isolate not used during immunization), and binds to cell surface -expressed gp160. These hybridomas will be made available to the scien tific community through a hybridoma culture facility.