1. ACE2-using coronaviruses: A global concern通信作者刘科芳、高福引用Xu Z, Lobato AC, Liu K, et al. ACE2-using coronaviruses: A global concern. hLife 2025; 3: 615–617.2. Enabling the immune escaped etesevimab fully-armed against SARS-CoV-2 Omicron subvariants including KP.2hLife | 中国科学院高福院士团队开发BAADesign赋能埃特司韦单抗破解新冠Omicron变异株挑战通信作者杨梦苏、高福引用Su C, He J, Xie Y, et al. Enabling the immune escaped etesevimab fully-armed against SARS-CoV-2 Omicron subvariants including KP.2. hLife 2025; 3: 132–145.3. H3N2 influenza virus characteristics in China (2019–2022): Genetic, antigenic, and infection dynamics during the COVID-19 pandemic中国科学院微生物所毕玉海团队在季节性流感病毒研究上取得进展通信作者张洪春、毕玉海引用Li J, Huan Y, Xia Q, et al. H3N2 influenzavirus characteristics in China (2019–2022): Genetic, antigenic, and infection dynamics during the COVID-19 pandemic. hLife 2025; 3: 146–158.4.Modeling viral evolution: A novel SIRSVIDE framework with application to SARS-CoV-2 dynamicshLife | 陆剑研究团队研发SIRSVIDE模型解析病毒进化动态通信作者陆剑本研究研发了SIRSVIDE Susceptible-Infected-Recovered-Susceptible-Variation-Immune Decay-Immune Escape 的新型计算模型用于模拟病毒种群的传播和进化动态。引用Jin K, Tang X, Qian Z, et al. Modeling viral evolution: A novel SIRSVIDE framework with application to SARS-CoV-2 dynamics. hLife 2024; 2: 227–245.5. Why is the Omicron main protease of SARS-CoV-2 less stable than its wild-type counterpart? A crystallographic, biophysical, and theoretical study通信作者Jana Shen、Rolf Hilgenfeld引用Ibrahim M, Sun X, Martins de Oliveira V, et al. Why is the Omicron main protease of SARS-CoV-2 less stable than its wild-type counterpart? A crystallographic, biophysical, and theoretical study. hLife 2024; 2: 419–433.6.Prophylactic and therapeutic itaconate treatment alleviates COVID-19-associated lung injury通信作者林树海、张天英、夏宁邵引用Jiang Y, Yang P, Yao B, et al. Prophylactic and therapeutic itaconate treatment alleviates COVID-19-associated lung injury. hLife 2025; 3: 551–564.7.Selection and engineering of broad-spectrum antiviral affibody peptides against SARS-CoV-2 variants通信作者Christopher John Hipolito、齐建勋、施一引用Yang J, Wang M, Chen Z, et al. Selection and engineering of broad-spectrum antiviral affibody peptides against SARS-CoV-2 variants. hLife 2025; 3: 448–451.8. Palmitic acid esters of hydroxy stearic acids suppress SARS-CoV-2 infection through inhibiting the non-canonical inflammasome通信作者夏朋延引用Kong C, Li Y, Qian Y, et al. Palmitic acid esters of hydroxy stearic acids suppress SARS-CoV-2 infection through inhibiting the non-canonical inflammasome. hLife 2025; 3: 452–454.9.Rational design of human CD26 receptor for a strong neutralizing ability against MjHKU4r-CoV-1 and MERS-CoV通信作者白崇智、苏超、韩鹏程A novel pangolin-origin Middle East respiratory syndrome coronavirus-like (MERS-like coronavirus), Manis javanica HKU4-related coronavirus 1 (MjHKU4r-CoV-1), has recently been identified. This virus utilizes dipeptidyl peptidase 4 (DPP4 or CD26) as its entry receptor and exhibits high infectivity in human cells and organs. However, no therapeutic agents have been developed to inhibit a potential outbreak of MjHKU4r-CoV-1. In this study, we determined the Cryo-electron microscopy (Cryo-EM) structure of the MjHKU4r-CoV-1 receptor-binding domain (RBD) in complex with human CD26 (hCD26), revealing the detailed interactions at the virus-receptor interface. Based on these structural insights, we designed an hCD26 mutant (hCD26mu) with enhanced binding affinity for the MjHKU4r-CoV-1 RBD and demonstrated its potent neutralizing activity against MjHKU4r-CoV-1 pseudovirus. When fused to ferritin as a nanoparticle, the hCD26mu exhibited increased neutralization potency against both MjHKU4r-CoV-1 and MERS-CoV. These findings highlight the potential of the optimized hCD26mu as a therapeutic candidate for preventing MjHKU4r-CoV-1 infection.引用Zhang Y, Tian M, Han Y, et al. Rational design of human CD26 receptor for a strong neutralizing ability against MjHKU4r-CoV-1 and MERS-CoV. hLife 2025; 3: 565–568.10.High-resolution crystal structure of human coronavirus HKU1 receptor binding domain bound to TMPRSS2 receptor通信作者陈蓉徐颖张水军This study presents the high-resolution structure of HCoV-HKU1A RBD bound to human TMPRSS2 receptor, which reveals the structural basis for the specificity of receptor binding by HCoV-HKU1. The interface between HCoV-HKU1 RBD and receptor also provides information for the development of vaccines and antivirals against HCoV-HKU1.引用Wang W, Guan J, Ren M, et al. High-resolution crystal structure of human coronavirus HKU1 receptor binding domain bound to TMPRSS2 receptor. hLife 2024; 2: 653–657.