Xiao Yi Sun's research while affiliated with Princess Alexandra Hospital (Queensland Health) and other places

Publications (6)

Article
Full-text available
Translation of mRNA encoding the L1 and L2 capsid proteins of papillomavirus (PV) is restricted in vivo to differentiated epithelial cells, although transcription of the L1 and L2 late genes occurs more widely. The codon composition of PV late genes is quite different from that of most mammalian genes. To test the possibility that PV late gene codo...
Article
The bovine papillomavirus type 1 (BPV1) L2 protein purified from Escherichia coli was used as an antigen to produce monoclonal antibodies (MAbs). A total of 26 individual clones which recognized the BPV1 L2 protein were obtained. Using infectious BPV1 virus particles, 3 of the MAbs were found to interact with BPV1 virus particles. Binding of the MA...
Article
We examined glycosylation of the L1 capsid protein of human papillomavirus type 16, using HPV16 L1 protein expressed from various recombinant vaccinia viruses in CV-1 and HaCaT cells. A minority of L1 protein was N-glycosylated, and all four potential N-glycosylation sites appeared to be used. Glycosylation was of the high-mannose type, as shown by...
Article
In certain circumstances, cells infected with vaccinia virus (VV) undergo fusion, but this does not occur in tissue cultures infected with wild-type VV. The VV genome includes three genes (B24R, B13R, and K2L) encoding polypeptides that are structurally related to members of the plasma serine protease inhibitor (SPI) superfamily. In this study, we...
Article
Human papillomavirus type 16(HPV16) L1 and L2 capsid proteins can be detected only in the nucleus of infected cells. For other nuclear proteins, specific sequences of basic amino acids(aa) termed nuclear localization signals (NLS) direct the protein from the cytoplasm to the nucleus. We used a series of deletion and substitution mutations of the HP...
Article
A recombinant vaccinia virus termed pLC201 VV was designed to coexpress the Li and L2 late genes of human papillomavirus type 16 (HPV16). Synthesis of the Li and L2 proteins occurred in cells infected with pLC201VV, and 40-nm virus-like particles with a density of 1.31 g/ml were produced in the nuclei of cells synthesizing both L1 and L2, but not i...

Citations

... Only upon MV being internalized into endosomes can the acidic environment of these organelles trigger conformational changes in the A26 protein to induce EFC fusion activation and subsequent viral membrane fusion with endosomes, releasing viral cores into the cytoplasm (29). Unlike A26, the A56/K2 protein complex is expressed on cell surfaces in the early stage of virus infection to inhibit EV-mediated fusion to infected cells in a process termed "superinfection interference" (25,(30)(31)(32)(33)(34)(35). Overexpression of A56 and K2 on the surfaces of HeLa cells was found to inhibit not only vaccinia EV cell entry but also MV entry (36). ...
... for virus assembly along with L1 and helps in transport of viral particles to the host cell nucleus. L2 protein also helps in mediating the increased efficiency of formation of VLPs by binding with L1 [31,32]. The C-terminal amino acid residues 396-439 of HPV11 L2 are shown to form the L1 binding domain [11,33]. ...
... At the C-termini of the L1 proteins, MfuPV1 and MfuPV2 have two NLSs, promoting the accumulation of L1 proteins in the cellular nucleus where they assemble into capsomeres and then into viral capsids [41,42]. In both novel PVs, the L2 protein contains a binding site for the L1 protein at its C-terminus, which enables the assembly of capsid proteins into capsomeres. ...
... In addition, swine is a significant animal reservoir of rotavirus P genotypes. Multiple genotypes, such as P [13], P [23], P [26], P [27], P [32] and P [34], infect only swine. In contrast, P[1], P [3], P [7], P [9], P [14], and P [19] infect humans and other animals including swine [22]. ...
... Although our results showed 4 conserved glycosylation positions in all sequences, based on previous studies we could not find any function for glycosylated regions. Zhou et al. in 1993 showed while the majority of L1 protein localizes in the cell nucleus, glycosylated L1 remains in the endoplasmic reticulum and it is not exported from the cell nor translocated to the cell membrane or the cell nucleus (Zhou et al. 1993). Therefore, they concluded that glycosylated L1 was not important in the construction of papillomavirus virion. ...
... CRPV capsids were more efficient for rabbit cells but comparable to HPV58 capsids in human cells. In agreement with previous studies [6,[15][16][17][18], we also demonstrated that the L2 protein plays a critical role that contributed to the efficiency of the delivery of attached DNA. Furthermore, we showed that PSVs with a papillomavirus genome showed better delivery of externally attached DNA when compared with PSVs with a plasmid DNA. ...