Yang Wenyu, Wang Liping, Shi Lei, Zhang Jialin, Liu Heidi, Wang Jun, Ma Wenjun
Department of Veterinary Pathobiology, College of Veterinary Medicine, University of Missouri, Columbia, MO 65211, USA.
Department of Molecular Microbiology and Immunology, School of Medicine, University of Missouri, Columbia, MO 65212, USA.
Pathogens. 2025 Jun 18;14(6):599. doi: 10.3390/pathogens14060599.
Novel bat influenza viruses show different features in contrast to classical influenza A viruses (IAVs). The M2 of IAVs functions as an ion channel that plays an important role in virus entry, viral assembly, and release and also serves as the antiviral target. To date, whether bat influenza M2 functions as the ion channel like classical IAV M2 remains unknown. Here, we show that the bat influenza M2 amino acid at position 31 (N/S) is critical for sensitivity to antivirals targeting the ion channel such as amantadine and other tested antivirals and that the amino acids at position 37 (H/G) and 41 (W/A) are crucial for virus replication and survival. The results indicate that bat influenza M2 functions similarly to conventional IAVs despite the low identity between the two.
与经典甲型流感病毒(IAV)相比,新型蝙蝠流感病毒具有不同的特征。IAV的M2作为一种离子通道,在病毒进入、病毒组装和释放过程中发挥重要作用,也是抗病毒靶点。迄今为止,蝙蝠流感M2是否像经典IAV M2一样发挥离子通道功能仍不清楚。在此,我们表明蝙蝠流感M2第31位氨基酸(N/S)对于对靶向离子通道的抗病毒药物(如金刚烷胺)及其他测试抗病毒药物的敏感性至关重要,并且第37位(H/G)和41位(W/A)氨基酸对于病毒复制和存活至关重要。结果表明,尽管两者之间的同源性较低,但蝙蝠流感M2的功能与传统IAV相似。