Advancing EBV Research: Harnessing LEXSY technology for BGLF4 protein kinase expression and discovery

LEXSY is a eukaryotic protein expression platform based on the S1-classified protozoan L. tarentolae, which has already been used for the expression of various viral proteins^[1-5].

A recent publication^[6] showed the significant role of the EBV-encoded protein kinase BGLF4 in viral replication and discusses its potential as a target for antiviral therapy, while also emphasizing the importance of continued research into its interactions and functions. The use of the LEXSY technology in expressing and purifying BGLF4 is crucial for advancing these studies by enabling efficient and reliable production of the protein for further analysis.

Figure 1: Indirect immunofluorescence staining of interactive complexes in EBV-positive cells using the antibodies directed against Leishmania-expressed BGLF4 (EBV-encoded protein kinase, located to the nucleus) and PDH (pyruvate dehydrogenase, distributed at non-nuclear locations). From Kögler et al. (2026)^[6].

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References:

[1] Fischer et al. (2016) Expression, characterisation and antigenicity of a truncated Hendra virus attachment protein expressed in the protozoan host Leishmania tarentolae. J. Virol. Methods 228:48.

[2] Czarnota et al. (2020) Specific Antibodies Induced by Immunization with Hepatitis B Virus-Like Particles Carrying Hepatitis C Virus Envelope Glycoprotein 2 Epitopes Show Differential Neutralization Efficiency. Vaccines 8:E294.

[3] Panasiuk et al. (2022) Chimeric virus-like particles presenting tumour-associated MUC1 epitope result in high titers of specific IgG antibodies in the presence of squalene oil-in-water adjuvant: towards safe cancer immunotherapy. J Nanobiotechnology 20:160.

[4] Zimna et al. (2024) Leishmania tarentolae as a platform for the production of vaccines against viral pathogens. NPJ Vaccines 9:212.

[5] Son et al. (2024) Efficient Expression in Leishmania tarentolae (LEXSY) of the Receptor-Binding Domain of the SARS-CoV-2 S-Protein and the Acetylcholine-Binding Protein from Lymnaea stagnalis. Molecules 29:943.

[6] Kögler et al. (2026) Identification of a New Phosphorylated Host Interactor of the Epstein–Barr Virus (EBV) Kinase BGLF4 Suggests Key Points for EBV-Specific Antiviral Drug Targeting. Int J Mol Sci. 27:2627.