Reingard Grabherr

As an antigenic target for capripoxvirus, we used the homolog of the vaccinia virus C-type lectin-like protein A34 (LSDV ORF 123). The expression and purification of the antigen were performed as previously described [28]. This recombinant antigen was successfully used in ELISA to detect antibodies against capripoxvirus in sheep, goats and cattle [28].

1. Introduction Protein glycosylation is a fundamental post-translational modification that is essential for various cellular functions such as cell adhesion, signaling, and immune responses. Various enzymes are responsible for proper biosynthesis and catabolism of specific glycans [1]. One important enzyme is the β-galactosidase (EC 3.2.1.23), which plays a crucial role in the hydrolysis of glycans containing terminal non-reducing β-D-galactose residues in β1,3-, β1,4- or β1,6-linkage [2].

PLOS ONE, Jul 2023 Due to comparably high product titers and low production costs, the baculovirus/insect cell expression system is considered a versatile production platform in the biopharmaceutical industry. Its excellence in producing complex multimeric protein assemblies, including virus-like particles (VLPs), which are considered promising vaccine candidates to counter emerging viral threats, made the system even more attractive.