Chinese hamster ovary (CHO) cell lines secreting a series of truncated forms of human immunodeficiency virus type 1 (HIV-1) IIIB (clone BH10) gp120 were assembled. Using purified glyco-proteins, we demonstrated the functional and structural integrity of these truncates by their reactivity with both sCD4 and anti-gp120 monoclonal antibodies (MAbs). Deletion of the V1, V2 and V3 regions had minimal effects on CD4 binding, but deletion of the NH terminus affected the folding of the truncated molecule. Deletion of either V1/V2 or V1/V2/V3 regions led to enhanced recognition by some, but not all, MAbs mapping to the CD4 binding site. In contrast, deletion of the V1/V2 regions had no effect on the ability of V3-specific MAbs to bind to the truncate. These results support the use of truncated forms of gp120 as components of potential HIV vaccines.


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