tailieunhanh - Báo cáo y học: "Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein | Wang et al. Virology Journal 2010 7 156 http content 7 1 156 VIROLOGY JOURNAL RESEARCH Open Access Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane protein Lei Wang Longding Liu Yanchun Che Lichun Wang Li Jiang Chenghong Dong Ying Zhang and Qihan Li Abstract HSV-1 viral capsid maturation and egress from the nucleus constitutes a self-controlled process of interactions between host cytoplasmic membrane proteins and viral capsid proteins. In this study a member of the tetraspanin superfamily CTMP-7 was shown to physically interact with HSV-1 protein VP26 and the VP26-CTMP-7 complex was detected both in vivo and in vitro. The interaction of VP26 with CTMP-7 plays an essential role in normal HSV-1 replication. Additionally analysis of a recombinant virus HSV-1-UG showed that mutating VP26 resulted in a decreased viral replication rate and in aggregation of viral mutant capsids in the nucleus. Together our data support the notion that biological events mediated by a VP26 - CTMP-7 interaction aid in viral capsid enveloping and egress from the cell during the HSV-1 infectious process. Background Herpes simplex virus type 1 HSV-1 is a double-stranded DNA virus with a 152 kb genome that has the capacity to encode more than 80 structural and non-structural viral proteins during its lifecycle in the cell 1 . Its structural proteins generate a dodecahedron protein capsid in the nucleus via their protein-protein interactions 2 . Despite the variety of capsid shapes 3 the basic general structures are composed of interior scaffold polypeptides principally VP22a VP21 viral protease VP24 and capsid shell proteins VP5 VP19c VP23 and VP26 4 . These proteins tend to assemble into viral capsid hexon and penton structures 5 through a specific mechanism that is not well understood. VP5 is the largest capsid protein and the major component of the capsid shell 6 while VP26 is the smallest capsid protein. VP26 localizes to the .