Recombinant antigens are antigenic proteins or protein-derived constructs produced through expression of engineered genetic sequences. Their molecular identity includes the encoded amino-acid sequence and any structural or chemical features introduced during biosynthesis. Glycosylation can contribute directly to recognized epitopes or influence the folding and accessibility of antigenic surfaces [1]. Recombinant expression can generate a selected antigenic protein as part of a larger fusion polypeptide [2]. The spatial arrangement of exposed residues establishes conformational epitopes recognized by antibodies, making folding and structural integrity integral properties of the expressed antigen [3]. Genetic fusion can also join an antigenic sequence to another protein domain within a single translation product [4].
- recombinant antigens
- protein expression
- antigenic determinants
- protein conformation
References
- Maddy L. Newby; Joel D. Allen; Max Crispin; Influence of glycosylation on the immunogenicity and antigenicity of viral immunogens. Biotechnol. Adv. 2023, 70, 108283, 10.1016/j.biotechadv.2023.108283.
- Dennis G. Kleid; Daniel Yansura; Barbara Small; Donald Dowbenko; Douglas M. Moore; Marvin J. Grubman; Peter D. McKercher; Donald O. Morgan; Betty H. Robertson; Howard L. Bachrach; et al. Cloned Viral Protein Vaccine for Foot-and-Mouth Disease: Responses in Cattle and Swine. Science 1981, 214, 1125-1129, 10.1126/science.6272395.
- Philip R. Dormitzer; Jeffrey B. Ulmer; Rino Rappuoli; Structure-based antigen design: a strategy for next generation vaccines. Trends Biotechnol. 2008, 26, 659-667, 10.1016/j.tibtech.2008.08.002.
- Peter Michael Moyle; Biotechnology approaches to produce potent, self-adjuvanting antigen-adjuvant fusion protein subunit vaccines. Biotechnol. Adv. 2017, 35, 375-389, 10.1016/j.biotechadv.2017.03.005.