Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.
Humabs Biomed SA, a subsidiary of Vir Biotechnology, 6500 Bellinzona, Switzerland.
Science. 2021 Aug 6;373(6555):648-654. doi: 10.1126/science.abi7994. Epub 2021 Jul 1.
A novel variant of concern (VOC) named CAL.20C (B.1.427/B.1.429), which was originally detected in California, carries spike glycoprotein mutations S13I in the signal peptide, W152C in the N-terminal domain (NTD), and L452R in the receptor-binding domain (RBD). Plasma from individuals vaccinated with a Wuhan-1 isolate-based messenger RNA vaccine or from convalescent individuals exhibited neutralizing titers that were reduced 2- to 3.5-fold against the B.1.427/B.1.429 variant relative to wild-type pseudoviruses. The L452R mutation reduced neutralizing activity in 14 of 34 RBD-specific monoclonal antibodies (mAbs). The S13I and W152C mutations resulted in total loss of neutralization for 10 of 10 NTD-specific mAbs because the NTD antigenic supersite was remodeled by a shift of the signal peptide cleavage site and the formation of a new disulfide bond, as revealed by mass spectrometry and structural studies.
一种名为 CAL.20C(B.1.427/B.1.429)的新型关注变异株,最初在加利福尼亚州被检测到,其刺突糖蛋白在信号肽中具有 S13I 突变、在 N 端结构域(NTD)中有 W152C 突变、在受体结合域(RBD)中有 L452R 突变。基于武汉-1 株的信使 RNA 疫苗接种个体或康复个体的血浆对 B.1.427/B.1.429 变异株的中和效价降低了 2-3.5 倍,与野生型假病毒相比。L452R 突变使 34 种 RBD 特异性单克隆抗体(mAb)中的 14 种的中和活性降低。S13I 和 W152C 突变导致 10 种 NTD 特异性 mAb 的中和活性完全丧失,因为信号肽切割位点的转移和新二硫键的形成重塑了 NTD 抗原超位,这一点通过质谱和结构研究得到了揭示。