Martínez-Flores Daniel, Rodríguez-Hernández Aaron Pavel, Sampieri Alicia, Cruz-Reséndiz Adolfo, Tobías-Juárez Ileana, Lara-Martínez Reyna, Jiménez-García Luis F, Vaca Luis
Departamento de Biología Celular y del Desarrollo, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad Universitaria, México City 04510, Mexico.
Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de México, Ciudad Universitaria, México City 04510, Mexico.
J Gen Virol. 2024 Dec;105(12). doi: 10.1099/jgv.0.002054.
Baculovirus is one of the most complex viruses found in nature. Proteomic analysis of budded viruses (BVs) indicates that they are formed by at least 50 different structural proteins. The function of most of these structural proteins and their specific localization in individual virions remain unknown. In the present study, we have conducted single-molecule localization microscopy analysis of the spatial distribution of the nucleocapsid protein P24 and the envelope proteins GP64 and E25. Our results show that P24 and GP64 are polarized to one end of the baculovirus, while E25 distributes more homogenously along the viral envelope. This is the first study using optical microscopy to demonstrate the polarized distribution of structural proteins in individual baculoviruses.
杆状病毒是自然界中发现的最复杂的病毒之一。对出芽病毒(BVs)的蛋白质组分析表明,它们由至少50种不同的结构蛋白组成。这些结构蛋白中的大多数的功能及其在单个病毒粒子中的特定定位仍然未知。在本研究中,我们对核衣壳蛋白P24以及包膜蛋白GP64和E25的空间分布进行了单分子定位显微镜分析。我们的结果表明,P24和GP64偏向杆状病毒的一端,而E25沿病毒包膜分布得更为均匀。这是第一项使用光学显微镜证明单个杆状病毒中结构蛋白极化分布的研究。