The oligogloopolymerization of rod-virus cortex protein GP41 is necessary for BV/ODV assembly

On April 12, the international academic journal Journal of Virology published the latest research results of Wang Hualin's team at the National Key Laboratory of Virology of the Wuhan Institute of Virology of the Chinese Academy of Sciences, entitled The functional oliric state of the teessentialgument protein 41 is for the baculovirus BV and ODV assembly ("The concentration of rod-like viral skin protein GP41 is necessary for BV/ODV assembly).
rod virus is a class of large DNA viruses that specifically infect insects, forming two different types of sub-viral particles during their infection cycle - bud-type virus particleBV and encapsulation virus particle ODV.
virus infects cells to replicate and assemble in the nucleus to form a nuclear shell, a part of the nuclear shell through the nuclear membrane transport to the cell membrane germination to form a BV, and another part of the nuclear shell left in the nucleus assembled into ODV, but the assembly mechanism of BV and ODV is not yet clear.
O-glycosylation modification is a kind of protein modification that is common in the biological world, o-glycosylation protein in cells usually plays an important role, mainly involved in regulating receptor binding, protein transport, signal transduction, nuclear hole complex formation and cytoskeleton formation.
and the function of the virus O-glycogen protein is still unclear.
GP41 is the only O-glycogen protein found in the rod virus, and studies have shown that it is rich in O-glycosyl modification, which is mainly located in the cortex structure between the ocsinoma and nuclear shell of ODV. Early studies
show that GP41 is involved in the nuclear transport of rod virus nuclear case and is therefore very important for BV formation, while GP41 is one of the main components of ODV, but whether it is involved in ODV formation is not clear.
researchers have for the first time explained the role of O-glycosylized viral protein GP41 in the proliferation of rod viruses by gene knockout.
study found that GP41 was involved in the nuclear transport of the BV nuclear case, and at the same time played an important role in the formation of ODV in the interaction between the nuclear shell and micro-follicles, and the absence of the gp41 gene led to the formation of both BV and ODV. at
the same time, GP41 forms oligomers during infection, where the triplepolymer is specifically packaged into the sub-viral particles BV and ODV, and it is assumed that the triplepolymer is a functional form of GP41.
further, it was discovered that the disulfur bond and the leucine zipper were the key structural sites for THE formation of the oligopolymer in GP41 (Figure 1).
this study provides an important basis for in-depth analysis of the role of rod virus O-glycogen in viral infection and the assembly mechanism of the virus (Figure 2). The first author of the
thesis is Li Yimeng, a doctoral student.
communication author is researcher Wang Hualin and associate researcher Wang Manli.
the research was supported by the Chinese Academy of Sciences' Strategic Leading Science and Technology Project (XDB11030400) and the National Natural Science Foundation Innovation Group Project (31621061).
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