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Abstract

Background: Japanese encephalitis virus (JEV), a member of the family Flaviviridae, is an important mosquito-borne human pathogen. Its envelope glycoprotein (E) is the major determinant of the pathogenicity and host immune responses. In the present study, we explored the feasibility of producing recombinant JEV E protein in the virus-free Drosophila expression system.

DENV-2 subunit proteins fused to CR2 receptor-binding domain (P28)-induces specific and neutralizing antibodies to the Dengue virus in mice

“…These events likely facilitate the generation of proteins that are similar to the wild-type proteins. 18,40 Cumulative studies have shown that both full-length C3d and the minimal P28 domain can be used as molecular adjuvants when fused to an antigen. Although our results did not demonstrate a significant difference in the neutralizing antibody response when recombinant proteins were fused to P28, the total level of antibodies against the native E protein increased (p < 0.01).…”

“…18 Domain III of DENV-2 expressed in this system was able to elicit a protective response in mice and monkeys. [19][20][21] Due to the low immunogenicity that the recombinant proteins in general possess, different strategies have been implemented to elicit a robust immune response against these antigens.…”

Proteins promote cancer nanotheranostics

“…However, the non-specific adsorption of nanoprobes is seriously affecting the detection accuracy and sensitivity. Leveraging on the unique domains and amino acid sequences of bio-endogenous proteins, some specific tactics, including surface engineering of nanoparticles with proteins, and protein-mediated biomimetic synthesis of nanoprobes have been developed in a green chemistry fashion in our group [1][2][3][4]. This protein-mediated cancer nanotheranostic strategy is of great significance in reducing nonspecific adsorption of nanoprobes for in vitro diagnosis and in vivo applications.…”

Glycoprotein E of the Japanese encephalitis virus forms virus-like particles and induces syncytia when expressed by a baculovirus

“…The crucial role of the interaction between prM and E has been well documented (Li et al, 2008;Lin & Wu, 2005;Zheng et al, 2010). Co-expression of prM and E has been successfully used to produce virus-like particles (VLPs) of flaviviruses, offering a promising approach to the production of vaccines and diagnostic antigens (Kojima et al, 2003;Konishi et al, 2001;Yamaji et al, 2012;Zhang et al, 2007). Moreover, this provides a model system for studying flavivirus envelope glycoprotein functions (Schalich et al, 1996).…”