Academic Journal
Immunogenicity Evaluation of N‑Glycans Recognized by HIV Broadly Neutralizing Antibodies
| العنوان: | Immunogenicity Evaluation of N‑Glycans Recognized by HIV Broadly Neutralizing Antibodies |
|---|---|
| المؤلفون: | Sachin S. Shivatare (1898056), Ting-Jen Rachel Cheng (2802103), Yang-Yu Cheng (1711639), Vidya S. Shivatare (6934592), Tsung-I Tsai (1711636), Hong-Yang Chuang (1898059), Chung-Yi Wu (151759), Chi-Huey Wong (63704) |
| سنة النشر: | 2021 |
| المجموعة: | Smithsonian Institution: Digital Repository |
| مصطلحات موضوعية: | Biophysics, Medicine, Microbiology, Ecology, Immunology, Cancer, Infectious Diseases, Virology, similar specificity pattern, identified novel hybrid, 9 , 5 , 3 , 2 , safe prophylactic vaccine, broadly neutralizing activities, glycan epitopes recognized, 1 positive patients, broadly neutralizing antibodies, chitobiose may interfere, modification may, like antibodies, various clades, vaccine development, type structures, results indicated, nontoxic mutant, nonspecific binding, improved treatment, igm response |
| الوصف: | While the improved treatment of human immunodeficiency virus type 1 (HIV-1) infection is available, the development of an effective and safe prophylactic vaccine against HIV-1 is still an unrealized goal. Encouragingly, the discovery of broadly neutralizing antibodies (bNAbs) from HIV-1 positive patients that are capable of neutralizing a broad spectrum of HIV-1 isolates of various clades has accelerated the progress of vaccine development in the past few years. Some of these bNAbs recognize the N-glycans on the viral surface gp120 glycoprotein. We have been interested in using the glycan epitopes recognized by bNAbs for the development of vaccines to elicit bNAb-like antibodies with broadly neutralizing activities. Toward this goal, we have identified novel hybrid-type structures with subnanomolar avidity toward several bNAbs including PG16, PGT121, PGT128-3C, 2G12, VRC13, VRC-PG05, VRC26.25, VRC26.09, PGDM1400, 35O22, and 10-1074. Here, we report the immunogenicity evaluation of a novel hybrid glycan conjugated to carrier DT CRM197 , a nontoxic mutant of the diphtheria toxin, for immunization in mice. Our results indicated that the IgG response was mainly against the chitobiose motif with nonspecific binding to a panel of N-glycans with reducing end GlcNAc–GlcNAc (chitobiose) printed on the glass slides. However, the IgM response was mainly toward the reducing end GlcNAc moiety. We further used the glycoconjugates of Man 3 GlcNAc 2 , Man 5 GlcNAc 2 , and Man 9 GlcNAc 2 glycans for immunization, and a similar specificity pattern was observed. These findings suggest that the immunogenicity of chitobiose may interfere with the outcome of N-glycan-based vaccines, and modification may be necessary to increase the immunogenicity of the entire N-glycan epitope. |
| نوع الوثيقة: | article in journal/newspaper |
| اللغة: | unknown |
| Relation: | https://figshare.com/articles/journal_contribution/Immunogenicity_Evaluation_of_N_Glycans_Recognized_by_HIV_Broadly_Neutralizing_Antibodies/16817417 |
| DOI: | 10.1021/acschembio.1c00375.s001 |
| الاتاحة: | https://doi.org/10.1021/acschembio.1c00375.s001 |
| Rights: | CC BY-NC 4.0 |
| رقم الانضمام: | edsbas.3522826 |
| قاعدة البيانات: | BASE |
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