Subjects: Biology >> Biophysics >> Biochemistry & Molecular Biology submitted time 2016-05-12
Abstract： The architecture and structural details of chromatin assembler, chromatin modifier, and chromatin remodeler, and their complexes with nucleosome and chromatin, are critical for revealing the molecular mechanisms for the establishment, maintenance and regulation of epigenetic information. The fast-developing cryo-electron microscopy (cryo-EM) provides an indispensible tool for the structure determiantion of the huge, multi-subunits, and flexible epigenetic regulation related macromolecular assemblies. In this review, we summarized the recent progresses on EM structural studies of macromolecules and complexes relating to epigenetic regulation.
Peer Review Status:
Awaiting Review
Subjects: Biology >> Biophysics >> Biology submitted time 2016-05-11
Abstract： Infectious bursal disease virus (IBDV) poses a significant threat to the poultry industry. Viral protein 2 (VP2), the major structural protein of IBDV, has been subjected to frequent mutations that have imparted tremendous genetic diversity to the virus. To determine how amino acid mutations may affect the virulence of IBDV, we built a structural model of VP2 of a very virulent strain of IBDV identified in China, vvIBDV Gx, and performed a molecular dynamics simulation of the interaction between virulence sites. The study showed that the amino acid substitutions that distinguish vvIBDV from attenuated IBDV (H253Q and T284A) favor a hydrophobic and flexible conformation of beta-barrel loops in VP2, which could promote interactions between the virus and potential IBDV-specific receptors. Population sequence analysis revealed that the IBDV strains prevalent in East Asia show a significant signal of positive selection at virulence sites 253 and 284. In addition, a signal of co-evolution between sites 253 and 284 was identified. These results suggest that changes in the virulence of IBDV may result from both the interaction and the co-evolution of multiple amino acid substitutions at virulence sites.
Peer Review Status:Awaiting Review
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