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首页> 外文期刊>Vaccine >Conformational constraints imposed on a pan-neutralizing HIV-1 antibody epitope result in increased antigenicity but not neutralizing response
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Conformational constraints imposed on a pan-neutralizing HIV-1 antibody epitope result in increased antigenicity but not neutralizing response

机译：泛中和HIV-1抗体表位的构象限制导致抗原性增加，但不中和反应

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摘要

2F5 is one of the few broadly neutralizing monoclonal antibodies against type 1 Human Immunodeficiency Virus (HIV-1). It recognizes the amino acid sequence ELDKWAS in gp41. We have previously identified a number of immunotargeting 2F5-reactive candidate immunogens. Three of them (designated H-BT1-3) have the ELDKWAS sequence constrained at beta-turn sites within the immunoglobulin heavy chain. Two others (L-CT and L-CTx3) have the sequence attached at the C-terminus of the immunoglobulin light chain with minimal conformational constraints. In the present investigation, the H-BTs were found to bind 2F5 with up to 10-fold higher affinities than their unconstrained counterpart. When used as immunogens, immunogen-specific antibodies were induced with or without adjuvant, confirming the immunotargeting potential of these immunogen constructs. While HIV-1 gp160 cross-reactive antibodies were induced, virus neutralization was not detected. Thus, factors other than 2F5 binding affinity may have a critical role to play in the design of a 2F5-based vaccine.
机译：2F5是为数不多的针对1型人类免疫缺陷病毒（HIV-1）的广泛中和的单克隆抗体之一。它识别gp41中的氨基酸序列ELDKWAS。我们先前已经确定了许多具有免疫靶向性的2F5反应性候选免疫原。其中三个（称为H-BT1-3）具有ELDKWAS序列，被限制在免疫球蛋白重链内的β-turn位点。另外两个（L-CT和L-CTx3）在免疫球蛋白轻链的C末端连接了序列，构象限制最小。在本研究中，发现H-BTs结合2F5的亲和力比不受约束的对应物高10倍。当用作免疫原时，可在有或没有佐剂的情况下诱导免疫原特异性抗体，从而证实了这些免疫原构建体的免疫靶向潜力。虽然诱导了HIV-1 gp160交叉反应抗体，但未检测到病毒中和。因此，2F5结合亲和力以外的因素可能在基于2F5的疫苗设计中起关键作用。

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