PEPTIDES MIMICKING SELECTED DISULFIDE LOOPS IN HIV-1 GP120, OTHER THAN V3, DO NOT ELICIT VIRUS-NEUTRALIZING ANTIBODIES
PEPTIDES MIMICKING SELECTED DISULFIDE LOOPS IN HIV-1 GP120, OTHER THAN V3, DO NOT ELICIT VIRUS-NEUTRALIZING ANTIBODIES
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DOI：
10.1089/aid.1991.7.657
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发表时间：
1991-08-01
影响因子：
1.5
通讯作者：
JIANG, SB
中科院分区：
文献类型：
--
作者：
NEURATH, AR;STRICK, N;JIANG, SB
The positions of all 9 intrachain disulfide bonds within the envelope glycoprotein gp120 of the human immunodeficiency virus (HIV-1) have been established recently. Peptides expected to mimic some of the disulfide-bonded domains [(120-133)-(203-221); (133-138)-(164-203); (224-254); (391-425) and (385-392)-(425-452)] were synthesized. All peptides, except (120-133)-(203-221), elicited in immunized rabbits relatively high levels of antibodies reacting with gp120 in enzyme-linked immunosorbent assay (ELISA) and/or Western immunoblot assays. However, these antibodies failed to neutralize the infectivity of HIV-1. Combined with earlier reports concerning other gp120 loop peptides, these results confirm the uniqueness of the V3 (303-338) loop in encompassing a principal determinant(s) involved in virus neutralization.
