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    Home > Biochemistry News > Biotechnology News > A multi-layered self-assembling body has been developed for the research and development of P22 virus-like particles.

    A multi-layered self-assembling body has been developed for the research and development of P22 virus-like particles.

    • Last Update: 2020-08-10
    • Source: Internet
    • Author: User
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    Virus-like particles (VLPs) are morphologically identical or similar to real viral particles, but because they do not have viral nucleic acids (DNA and RNA), they are just hollow particles containing a certain viral protein.
    because the virus-like particles are not infectious, as an immunogen, can be transmitted to immune cells in the same way as viral infection, effectively inducing the body's immune system to produce an immune protective response.
    , its structure and antigen epitope are very similar to natural viruses, have strong immunogenicity and good safety, which provides convenient for the basic research of viruses (gene therapy, drug therapy, etc.) and the development of vaccines.
    virus shell protein has a natural self-assembly ability, can effectively self-assemble in the eukaryokarita system, the virus-like particles of this self-assembling nature also makes it a highly self-assembled main material.
    Recently, Professor Trevor Douglas of the University of India developed a multi-layered self-assembling body through the research and development of P22 virus-like particles.
    the assembly consists of P22 virus-like particles loaded with multiple spider proteins and is stimulating lysate with pH and ion strength (Figure 1).
    the results were published in "Chemistry of The Materials" (DOI: 10.1021/acs.chemmater.7b04964) under the title "Stimuli Responsive Hierarchical Assembly of P22 Virus-like Particles".
    in order to make the P22 virus-like particle assembly responsive to the pH of the solution, the authors designed and synthesized a fusion protein (Dec-Spider Silk Protein, Dec-Ss, Figure 1a), which consists of three parts: the green tripolymer can Combined with the surface of viral-like particles, and with different junction strength, the beige part is a stimulating and responsive spider protein, which forms a dipolymer in an environment with a pH of less than 6.5, and the middle blue part is a flexible connection chain.
    through this design, The P22 virus-like particles loaded with Dec-S will be present in the form of an assembly body at a lower pH (Figure 2b), and after gradually raising the pH, the dipolymers between Dec-Ss continue to disassemble, and eventually P22 virus-like particles will be present in monomer form (Figure 2b).
    the authors also found that low concentrations of Dec-Ss in the solution inhibit editing of virus-like particles, while high-concentration Dec-Ss increases the size of the assembly.
    the authors speculate that this is because at low concentrations, free Dec-Ss in the solution compete seis on the surface of the virus-like particles to form dipolymers, while at high concentrations, Dec-Ss on the surface of viral-like particles that do not form dipolymers will participate in the formation of assemblies with the help of free Dec-Ss, thereby increasing the size of the assembly body (Figure 2c).
    because P22 virus-like particles have a strong electronegativeness, they spontaneously form assemblies through charge interactions with positively charged compounds in the solution.
    in addition to the response to the pH, the authors also studied the responsiveness of p22 virus-like particle assembly to ion intensity through a green fluorescent protein with 36 positive charges (GFP (plus 36)," and the NaCl concentration of 125 mM is a critical value for viral-sampled particle assemblies in a solution where GFP is now present.
    virus-like particles are present in the form of assembled bodies at
    below this concentration, while above this concentration are in the form of monomers.
    also found that the assembly behavior of this virus-like particles can be regulated simultaneously by pH and ion strength (Figure 3).
    .
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