Rusche J R, Javaherian K, McDanal C, Petro J, Lynn D L, Grimaila R, Langlois A, Gallo R C, Arthur L O, Fischinger P J
Repligen Corporation, Cambridge, MA 02139.
Proc Natl Acad Sci U S A. 1988 May;85(9):3198-202. doi: 10.1073/pnas.85.9.3198.
Antisera to recombinant human immunodeficiency virus (HIV) proteins containing the entire envelope, gp160, or the central portion of the envelope, PB1, can inhibit fusion of virally infected cells in culture. This fusion inhibition is HIV-variant specific--that is, anti-gp160-IIIB inhibits fusion of isolate HTLV-IIIB-infected cells but not of isolate HTLV-IIIRF-infected cells. Both anti-gp160 and anti-PB1 are completely blocked in fusion inhibition activity by the addition of PB1 protein. A 24-amino acid peptide (RP135, amino acids 307-330) completely blocks fusion inhibition activity of both antisera and also blocks the activity of serum from a chimpanzee infected with HTLV-IIIB. Thus, the principal epitope that elicits fusion-inhibiting antibodies is located in the central portion of gp120.
针对包含完整包膜蛋白gp160或包膜中央部分PB1的重组人类免疫缺陷病毒(HIV)蛋白的抗血清,可抑制培养物中病毒感染细胞的融合。这种融合抑制具有HIV变体特异性,即抗gp160-IIIB可抑制分离株HTLV-IIIB感染细胞的融合,但不能抑制分离株HTLV-IIIRF感染细胞的融合。添加PB1蛋白后,抗gp160和抗PB1的融合抑制活性均被完全阻断。一种24个氨基酸的肽(RP135,氨基酸307 - 330)可完全阻断两种抗血清的融合抑制活性,也可阻断感染HTLV-IIIB的黑猩猩血清的活性。因此,引发融合抑制抗体的主要表位位于gp120的中央部分。