Laboratory of Microfluidic Technologies for Biomedicine, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia.
Faculty of Biology and Biotechnology, National Research University Higher School of Economics, Moscow, Russia.
Dokl Biochem Biophys. 2022 Dec;507(1):298-301. doi: 10.1134/S1607672922060084. Epub 2023 Feb 14.
In this work, we analyzed the binding affinities of mutated peptides of Omicron strain variants BA.1-BA.5 and the worldwide prevalent HLA alleles. Bioinformatics analysis was conducted with the use of T-CoV web portal. We showed that, for all five viral variants, mutations cause a significant reduction in the number of tightly binding peptides for HLA-B07:02 and HLA-C01:02 molecules. At the same time, there were novel potential mutant epitopes (binding affinity less than 50 nM) in case of HLA-A32:01 allele. Interestingly, mutations caused multidirectional effect on the binding affinities of the viral peptides and HLA-DRB103:01. Specifically, Spike protein mutations in the BA.1 variant caused more than 100-fold decrease in PINLVRDLPQGFSAL binding affinity, 10-fold decrease in affinity in the case of BA.2, BA.4, and BA.5 variants, and 30% increase in affinity for the BA.3 variant.
在这项工作中，我们分析了奥密克戎变异株 BA.1-BA.5 的突变肽与全球流行的 HLA 等位基因的结合亲和力。使用 T-CoV 门户网站进行了生物信息学分析。我们表明，对于所有五种病毒变异株，突变导致与 HLA-B07:02 和 HLA-C01:02 分子紧密结合的肽数量显著减少。同时，在 HLA-A32:01 等位基因的情况下，存在新的潜在突变表位（结合亲和力小于 50 nM）。有趣的是，突变对病毒肽和 HLA-DRB103:01 的结合亲和力产生了多向影响。具体来说，BA.1 变异株的 Spike 蛋白突变导致 PINLVRDLPQGFSAL 结合亲和力降低了 100 多倍，BA.2、BA.4 和 BA.5 变异株的亲和力降低了 10 倍，而 BA.3 变异株的亲和力增加了 30%。
