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Viral proteins expressed in LEXSY

Viral proteins are often difficult to express in bacterial expression systems due to misfolding or missing glycosylation. The eukaryotic expression system LEXSY is especially well-suited for the expression of viral proteins with correct folding and antigen activity (see Figure 1 and Table 1).

Figure 1: LEXSY cells expressing the E1E2 complex of hepatitis C virus envelope proteins (green). From Grzyb et al., 2016.
Figure 1: LEXSY cells expressing the E1E2 complex of hepatitis C virus envelope proteins (green). From Grzyb et al., 2016[2].

Table 1: Selection of viral proteins expressed with LEXSY.

Viral protein References
Hepatitis C core protein Bolhassani et al., 2017[1]
Hepatitis C E1E2 complex Grzyb et al., 2016[2]
Hepatitis C sHBsAg protein Czarnota et al., 2016[3]
Hendra attachment protein Fischer et al., 2016[4]
Hepatitis E capsid protein Baechlein et al., 2013[5]
Dr. Andreas Licht

Need further information? Please check out the LEXSY section or contact Andreas by email at expression@jenabioscience.com!

References:

[1] Bolhassani et al. (2017) Comparison of HCV Core and CoreE1E2 Virus-Like Particles Generated by Stably Transfected Leishmania tarentolae for the Stimulation of Th1 Immune Responses in Mice. Curr. Drug Deliv. 14:1040.
[2] Grzyb et al. (2016) Immunogenicity and functional characterization of Leishmania-derived hepatitis C virus envelope glycoprotein complex. Sci. Rep. 6:30627.
[3] Czarnota et al. (2016) Immunogenicity of Leishmania-derived hepatitis B small surface antigen particles exposing highly conserved E2 epitope of hepatitis C virus. Microb. Cell Fact. 15:62.
[4] 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.
[5] Baechlein et al. (2013) Expression of a truncated hepatitis E virus capsid protein in the protozoan organism Leishmania tarentolae and its application in a serological assay. J. Virol. Methods 193:238.