SplitCore Technology Allows Efficient Production of Virus-Like Particles Presenting a Receptor-Contacting Epitope of Human IgE

Baltabekova, A.Zh.; Shagyrova, Zh. S.; Kamzina, Aigerim S.; Voykov, M.; Zhiyenbay, Ye.; Ramanculov, Erlan; Shustov, Alexandr V.

doi:10.1007/s12033-015-9867-0

Cited by 10 publications

(7 citation statements)

References 38 publications

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“…However, the genetic integration of foreign epitopes into the core protein is limited in terms of the length and structure of the insert which can be incorporated before negatively influencing VLP assembly, stability, solubility as well as correct antigen folding 20 – 22 . While different strategies, including mosaic particles 21 , 23 , 24 , the split core 25 – 27 and tandem core 28 technology, have been developed to allow insertion of larger and structurally more complex proteins, steric hindrance is still a limiting factor. An alternative that can avoid this is chemical conjugation 29 .…”

Section: Introductionmentioning

confidence: 99%

Covalent protein display on Hepatitis B core-like particles in plants through the in vivo use of the SpyTag/SpyCatcher system

Peyret

Ponndorf

Meshcheriakova

et al. 2020

Sci Rep

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Virus-like particles (VLPs) can be used as nano-carriers and antigen-display systems in vaccine development and therapeutic applications. Conjugation of peptides or whole proteins to VLPs can be achieved using different methods such as the SpyTag/SpyCatcher system. Here we investigate the conjugation of tandem Hepatitis B core (tHBcAg) VLPs and the model antigen GFP in vivo in Nicotiana benthamiana. We show that tHBcAg VLPs could be successfully conjugated with GFP in the cytosol and ER without altering VLP formation or GFP fluorescence. Conjugation in the cytosol was more efficient when SpyCatcher was displayed on tHBcAg VLPs instead of being fused to GFP. This effect was even more obvious in the ER, showing that it is optimal to display SpyCatcher on the tHBcAg VLPs and SpyTag on the binding partner. To test transferability of the GFP results to other antigens, we successfully conjugated tHBcAg VLPs to the HIV capsid protein P24 in the cytosol. This work presents an efficient strategy which can lead to time and cost saving post-translational, covalent conjugation of recombinant proteins in plants.

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Section: Introductionmentioning

confidence: 99%

Covalent protein display on Hepatitis B core-like particles in plants through the in vivo use of the SpyTag/SpyCatcher system

Peyret

Ponndorf

Meshcheriakova

et al. 2020

Sci Rep

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“…Such a tandemly fused HBsAg dimer can form VLP in bacteria and plants and can enhance the capacity of accommodating foreign proteins at the major insertion region (MIR). Similarly, a HBcAg carrier was developed by the assembly of two polypeptide chains carrying an FG loop from a third domain of immunoglobulin E (IgE) heavy chain which can efficiently form VLPs (SplitCore technology) [23]. Such a method can elicit human IgE antibodies.…”

Section: Virus-like Particles (Vlps)mentioning

confidence: 99%

The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design

Nguyễn

Kikuchi

Maity

et al. 2021

IJMS

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Protein assemblies provide unique structural features which make them useful as carrier molecules in biomedical and chemical science. Protein assemblies can accommodate a variety of organic, inorganic and biological molecules such as small proteins and peptides and have been used in development of subunit vaccines via display parts of viral pathogens or antigens. Such subunit vaccines are much safer than traditional vaccines based on inactivated pathogens which are more likely to produce side-effects. Therefore, to tackle a pandemic and rapidly produce safer and more effective subunit vaccines based on protein assemblies, it is necessary to understand the basic structural features which drive protein self-assembly and functionalization of portions of pathogens. This review highlights recent developments and future perspectives in production of non-viral protein assemblies with essential structural features of subunit vaccines.

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“…Some of the most powerful approaches to interfere with IgE‐associated allergies are those that target IgE, their specific receptors (FcεRs), and/or IgE‐producing B cells/plasma cells directly . These treatment modalities intend to remove IgE‐producing cells themselves or to neutralize the effector function of IgE.…”

Section: Vnp‐based Strategies For Allergy Treatmentmentioning

confidence: 99%

“…Notably, the antibodies induced in rats blocked the binding of soluble rat IgE to rat FcεR and also downregulated rat serum IgE‐antibody levels; however, they did not react with FcεR‐bound rat IgE, demonstrating the safety (non‐anaphylactogenicity) of the induced autoantibodies. The split core technology , which allows for the expression of structural epitopes on the surface of hepatitis B particles (HBcAg), was used to generate blocking antibodies, which specifically target the receptor‐contacting site of the human C3ε domain of IgE . Immunization of mice with such IgE‐epitope‐HBcAg particles induced high‐titer (>1:36 000) anti‐human IgE antibodies .…”

Section: Vnp‐based Strategies For Allergy Treatmentmentioning

confidence: 99%

“…The split core technology , which allows for the expression of structural epitopes on the surface of hepatitis B particles (HBcAg), was used to generate blocking antibodies, which specifically target the receptor‐contacting site of the human C3ε domain of IgE . Immunization of mice with such IgE‐epitope‐HBcAg particles induced high‐titer (>1:36 000) anti‐human IgE antibodies . Another study showed that human IgE can even be targeted in its transmembrane form, as expressed on human IgE‐producing B cells/plasma cells, and without simultaneously targeting receptor‐bound IgE.…”

Section: Vnp‐based Strategies For Allergy Treatmentmentioning

confidence: 99%

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All the small things: How virus‐like particles and liposomes modulate allergic immune responses

et al. 2019

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Recent years have seen a dramatic increase in the range of applications of virus‐like nanoparticle (VNP)‐ and liposome‐based antigen delivery systems for the treatment of allergies. These platforms rely on a growing number of inert virus‐backbones or distinct lipid formulations and intend to engage the host's innate and/or adaptive immune system by virtue of their co‐delivered immunogens. Due to their particulate nature, VNP and liposomal preparations are also capable of breaking tolerance against endogenous cytokines, Igs, and their receptors, allowing for the facile induction of anti‐cytokine, anti‐IgE, or anti‐FcεR antibodies in the host. We here discuss the “pros and cons” of inducing such neutralizing autoantibodies. Moreover, we cover another major theme of the last years, i.e., the engineering of non‐anaphylactogenic particles and the elucidation of the parameters relevant for the specific trafficking and processing of such particles in vivo. Finally, we put the various technical advances in VNP‐ and liposome‐research into (pre‐)clinical context by referring and critically discussing the relevant studies performed to treat allergic diseases.

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SplitCore Technology Allows Efficient Production of Virus-Like Particles Presenting a Receptor-Contacting Epitope of Human IgE

Cited by 10 publications

References 38 publications

Covalent protein display on Hepatitis B core-like particles in plants through the in vivo use of the SpyTag/SpyCatcher system

Covalent protein display on Hepatitis B core-like particles in plants through the in vivo use of the SpyTag/SpyCatcher system

The Versatile Manipulations of Self-Assembled Proteins in Vaccine Design

All the small things: How virus‐like particles and liposomes modulate allergic immune responses

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