Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate
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<i>β</i> conjugates as a mimic of the propo...
Guardado en:
| Autores principales: | , , , , |
|---|---|
| Formato: | article |
| Lenguaje: | EN |
| Publicado: |
MDPI AG
2021
|
| Materias: | |
| Acceso en línea: | https://doaj.org/article/282b58a8d3e447fe8c113391fbbbb5e3 |
| Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
| id |
oai:doaj.org-article:282b58a8d3e447fe8c113391fbbbb5e3 |
|---|---|
| record_format |
dspace |
| spelling |
oai:doaj.org-article:282b58a8d3e447fe8c113391fbbbb5e32021-11-25T17:57:37ZChemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate10.3390/ijms2222125381422-00671661-6596https://doaj.org/article/282b58a8d3e447fe8c113391fbbbb5e32021-11-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/22/12538https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067The 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<i>β</i> 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<i>β</i>), 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<i>β</i>-conjugates for antibody PG9 was dependent on the density of the glycopeptide antigen display. The glycopeptide-Q<i>β</i> conjugates synthesized represent a promising candidate of HIV-1 vaccine.Guanghui ZongChristian ToonstraQiang YangRoushu ZhangLai-Xi WangMDPI AGarticleglycopeptideglycoconjugateneutralizing epitopebacteriophage Q<i>β</i>neutralizing antibodyHIV vaccineBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 12538, p 12538 (2021) |
| institution |
DOAJ |
| collection |
DOAJ |
| language |
EN |
| topic |
glycopeptide glycoconjugate neutralizing epitope bacteriophage Q<i>β</i> neutralizing antibody HIV vaccine Biology (General) QH301-705.5 Chemistry QD1-999 |
| spellingShingle |
glycopeptide glycoconjugate neutralizing epitope bacteriophage Q<i>β</i> neutralizing antibody HIV vaccine Biology (General) QH301-705.5 Chemistry QD1-999 Guanghui Zong Christian Toonstra Qiang Yang Roushu Zhang Lai-Xi Wang Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate |
| description |
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<i>β</i> 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<i>β</i>), 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<i>β</i>-conjugates for antibody PG9 was dependent on the density of the glycopeptide antigen display. The glycopeptide-Q<i>β</i> conjugates synthesized represent a promising candidate of HIV-1 vaccine. |
| format |
article |
| author |
Guanghui Zong Christian Toonstra Qiang Yang Roushu Zhang Lai-Xi Wang |
| author_facet |
Guanghui Zong Christian Toonstra Qiang Yang Roushu Zhang Lai-Xi Wang |
| author_sort |
Guanghui Zong |
| title |
Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate |
| title_short |
Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate |
| title_full |
Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate |
| title_fullStr |
Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate |
| title_full_unstemmed |
Chemoenzymatic Synthesis and Antibody Binding of HIV-1 V1/V2 Glycopeptide-Bacteriophage Q<i>β</i> Conjugates as a Vaccine Candidate |
| title_sort |
chemoenzymatic synthesis and antibody binding of hiv-1 v1/v2 glycopeptide-bacteriophage q<i>β</i> conjugates as a vaccine candidate |
| publisher |
MDPI AG |
| publishDate |
2021 |
| url |
https://doaj.org/article/282b58a8d3e447fe8c113391fbbbb5e3 |
| work_keys_str_mv |
AT guanghuizong chemoenzymaticsynthesisandantibodybindingofhiv1v1v2glycopeptidebacteriophageqibiconjugatesasavaccinecandidate AT christiantoonstra chemoenzymaticsynthesisandantibodybindingofhiv1v1v2glycopeptidebacteriophageqibiconjugatesasavaccinecandidate AT qiangyang chemoenzymaticsynthesisandantibodybindingofhiv1v1v2glycopeptidebacteriophageqibiconjugatesasavaccinecandidate AT roushuzhang chemoenzymaticsynthesisandantibodybindingofhiv1v1v2glycopeptidebacteriophageqibiconjugatesasavaccinecandidate AT laixiwang chemoenzymaticsynthesisandantibodybindingofhiv1v1v2glycopeptidebacteriophageqibiconjugatesasavaccinecandidate |
| _version_ |
1718411790961868800 |