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Issue 24, 2018
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Antimicrobial glycoconjugate vaccines: an overview of classic and modern approaches for protein modification

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Abstract

Glycoconjugate vaccines obtained by chemical linkage of a carbohydrate antigen to a protein are part of routine vaccinations in many countries. Licensed antimicrobial glycan–protein conjugate vaccines are obtained by random conjugation of native or sized polysaccharides to lysine, aspartic or glutamic amino acid residues that are generally abundantly exposed on the protein surface. In the last few years, the structural approaches for the definition of the polysaccharide portion (epitope) responsible for the immunological activity has shown potential to aid a deeper understanding of the mode of action of glycoconjugates and to lead to the rational design of more efficacious and safer vaccines. The combination of technologies to obtain more defined carbohydrate antigens of higher purity and novel approaches for protein modification has a fundamental role. In particular, methods for site selective glycoconjugation like chemical or enzymatic modification of specific amino acid residues, incorporation of unnatural amino acids and glycoengineering, are rapidly evolving. Here we discuss the state of the art of protein engineering with carbohydrates to obtain glycococonjugates vaccines and future perspectives.

Graphical abstract: Antimicrobial glycoconjugate vaccines: an overview of classic and modern approaches for protein modification

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Publication details

The article was received on 12 Jun 2018 and first published on 02 Oct 2018


Article type: Tutorial Review
DOI: 10.1039/C8CS00495A
Citation: Chem. Soc. Rev., 2018,47, 9015-9025
  • Open access: Creative Commons BY-NC license
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    Antimicrobial glycoconjugate vaccines: an overview of classic and modern approaches for protein modification

    F. Berti and R. Adamo, Chem. Soc. Rev., 2018, 47, 9015
    DOI: 10.1039/C8CS00495A

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