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APE-Gen2.0:将快速 I 类肽-主要组织相容性复合物建模扩展到翻译后修饰和非典型肽结构。

APE-Gen2.0: Expanding Rapid Class I Peptide-Major Histocompatibility Complex Modeling to Post-Translational Modifications and Noncanonical Peptide Geometries.

机构信息

Department of Computer Science, Rice University, Houston, Texas 77005, United States.

Department of Melanoma Medical Oncology─Research, The University of Texas MD Anderson Cancer Center, Houston, Texas 77054, United States.

出版信息

J Chem Inf Model. 2024 Mar 11;64(5):1730-1750. doi: 10.1021/acs.jcim.3c01667. Epub 2024 Feb 28.

Abstract

The recognition of peptides bound to class I major histocompatibility complex (MHC-I) receptors by T-cell receptors (TCRs) is a determinant of triggering the adaptive immune response. While the exact molecular features that drive the TCR recognition are still unknown, studies have suggested that the geometry of the joint peptide-MHC (pMHC) structure plays an important role. As such, there is a definite need for methods and tools that accurately predict the structure of the peptide bound to the MHC-I receptor. In the past few years, many pMHC structural modeling tools have emerged that provide high-quality modeled structures in the general case. However, there are numerous instances of non-canonical cases in the immunopeptidome that the majority of pMHC modeling tools do not attend to, most notably, peptides that exhibit non-standard amino acids and post-translational modifications (PTMs) or peptides that assume non-canonical geometries in the MHC binding cleft. Such chemical and structural properties have been shown to be present in neoantigens; therefore, accurate structural modeling of these instances can be vital for cancer immunotherapy. To this end, we have developed APE-Gen2.0, a tool that improves upon its predecessor and other pMHC modeling tools, both in terms of modeling accuracy and the available modeling range of non-canonical peptide cases. Some of the improvements include (i) the ability to model peptides that have different types of PTMs such as phosphorylation, nitration, and citrullination; (ii) a new and improved anchor identification routine in order to identify and model peptides that exhibit a non-canonical anchor conformation; and (iii) a web server that provides a platform for easy and accessible pMHC modeling. We further show that structures predicted by APE-Gen2.0 can be used to assess the effects that PTMs have in binding affinity in a more accurate manner than just using solely the sequence of the peptide. APE-Gen2.0 is freely available at https://apegen.kavrakilab.org.

摘要

T 细胞受体 (TCR) 识别与 I 类主要组织相容性复合体 (MHC-I) 受体结合的肽是触发适应性免疫反应的决定因素。虽然驱动 TCR 识别的确切分子特征仍不清楚,但研究表明,肽-MHC(pMHC) 结构的几何形状起着重要作用。因此,确实需要能够准确预测与 MHC-I 受体结合的肽结构的方法和工具。在过去的几年中,出现了许多 pMHC 结构建模工具,它们在一般情况下提供高质量的模拟结构。然而,在免疫肽组中有许多非典型情况,大多数 pMHC 建模工具都没有注意到,最值得注意的是,那些表现出非标准氨基酸和翻译后修饰 (PTM) 的肽,或者在 MHC 结合裂隙中呈现非典型几何形状的肽。这些化学和结构特性已被证明存在于新抗原中;因此,对这些情况进行准确的结构建模对于癌症免疫疗法至关重要。为此,我们开发了 APE-Gen2.0,它在建模准确性和非典型肽情况的可用建模范围方面都优于其前身和其他 pMHC 建模工具。一些改进包括:(i) 能够对具有不同类型 PTM(如磷酸化、硝化和瓜氨酸化)的肽进行建模;(ii) 一种新的和改进的锚定识别例程,用于识别和建模表现出非典型锚定构象的肽;以及 (iii) 一个提供易于访问的 pMHC 建模平台的网络服务器。我们进一步表明,APE-Gen2.0 预测的结构可用于更准确地评估 PTM 在结合亲和力方面的影响,而不仅仅是仅使用肽的序列。APE-Gen2.0 可在 https://apegen.kavrakilab.org 免费获得。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/cac5/10936522/aa17b3f975aa/ci3c01667_0001.jpg

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