Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q β Conjugates as a Vaccine Candidate.

Autor: Zong G; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA., Toonstra C; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA., Yang Q; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA., Zhang R; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA., Wang LX; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.
Jazyk: angličtina
Zdroj: International journal of molecular sciences [Int J Mol Sci] 2021 Nov 21; Vol. 22 (22). Date of Electronic Publication: 2021 Nov 21.
DOI: 10.3390/ijms222212538
Abstrakt: The broadly neutralizing antibody PG9 recognizes a unique glycopeptide epitope in the V1V2 domain of HIV-1 gp120 envelope glycoprotein. The present study describes the design, synthesis, and antibody-binding analysis of HIV-1 V1V2 glycopeptide-Q β conjugates as a mimic of the proposed neutralizing epitope of PG9. The glycopeptides were synthesized using a highly efficient chemoenzymatic method. The alkyne-tagged glycopeptides were then conjugated to the recombinant bacteriophage (Q β ), a virus-like nanoparticle, through a click reaction. Antibody-binding analysis indicated that the synthetic glycoconjugates showed significantly enhanced affinity for antibody PG9 compared with the monomeric glycopeptides. It was also shown that the affinity of the Q β -conjugates for antibody PG9 was dependent on the density of the glycopeptide antigen display. The glycopeptide-Q β conjugates synthesized represent a promising candidate of HIV-1 vaccine.
Databáze: MEDLINE
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