HIV-1 Envelope Glycosylation and the Signal Peptide
The RV144 trial represents the only vaccine trial to demonstrate any protective effect against HIV-1 infection. While the reason(s) for this protection are still being evaluated, it serves as justification for widespread efforts aimed at developing new, more effective HIV-1 vaccines. Advances in our...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-02-01
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| Series: | Vaccines |
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| Online Access: | https://www.mdpi.com/2076-393X/9/2/176 |
| _version_ | 1827588822239543296 |
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| author | Gregory S. Lambert Chitra Upadhyay |
| author_facet | Gregory S. Lambert Chitra Upadhyay |
| author_sort | Gregory S. Lambert |
| collection | DOAJ |
| description | The RV144 trial represents the only vaccine trial to demonstrate any protective effect against HIV-1 infection. While the reason(s) for this protection are still being evaluated, it serves as justification for widespread efforts aimed at developing new, more effective HIV-1 vaccines. Advances in our knowledge of HIV-1 immunogens and host antibody responses to these immunogens are crucial to informing vaccine design. While the envelope (Env) protein is the only viral protein present on the surface of virions, it exists in a complex trimeric conformation and is decorated with an array of variable N-linked glycans, making it an important but difficult target for vaccine design. Thus far, efforts to elicit a protective humoral immune response using structural mimics of native Env trimers have been unsuccessful. Notably, the aforementioned N-linked glycans serve as a component of many of the epitopes crucial for the induction of potentially protective broadly neutralizing antibodies (bnAbs). Thus, a greater understanding of Env structural determinants, most critically Env glycosylation, will no doubt be of importance in generating effective immunogens. Recent studies have identified the HIV-1 Env signal peptide (SP) as an important contributor to Env glycosylation. Further investigation into the mechanisms by which the SP directs glycosylation will be important, both in the context of understanding HIV-1 biology and in order to inform HIV-1 vaccine design. |
| first_indexed | 2024-03-09T00:44:06Z |
| format | Article |
| id | doaj.art-c842732071814343b5951eb6d271ed9e |
| institution | Directory Open Access Journal |
| issn | 2076-393X |
| language | English |
| last_indexed | 2024-03-09T00:44:06Z |
| publishDate | 2021-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Vaccines |
| spelling | doaj.art-c842732071814343b5951eb6d271ed9e2023-12-11T17:40:02ZengMDPI AGVaccines2076-393X2021-02-019217610.3390/vaccines9020176HIV-1 Envelope Glycosylation and the Signal PeptideGregory S. Lambert0Chitra Upadhyay1Division of Infectious Diseases, Department of Medicine, Icahn School of Medicine at Mount Sinai, 1 Gustave L. Levy Place, New York, NY 10029, USADivision of Infectious Diseases, Department of Medicine, Icahn School of Medicine at Mount Sinai, 1 Gustave L. Levy Place, New York, NY 10029, USAThe RV144 trial represents the only vaccine trial to demonstrate any protective effect against HIV-1 infection. While the reason(s) for this protection are still being evaluated, it serves as justification for widespread efforts aimed at developing new, more effective HIV-1 vaccines. Advances in our knowledge of HIV-1 immunogens and host antibody responses to these immunogens are crucial to informing vaccine design. While the envelope (Env) protein is the only viral protein present on the surface of virions, it exists in a complex trimeric conformation and is decorated with an array of variable N-linked glycans, making it an important but difficult target for vaccine design. Thus far, efforts to elicit a protective humoral immune response using structural mimics of native Env trimers have been unsuccessful. Notably, the aforementioned N-linked glycans serve as a component of many of the epitopes crucial for the induction of potentially protective broadly neutralizing antibodies (bnAbs). Thus, a greater understanding of Env structural determinants, most critically Env glycosylation, will no doubt be of importance in generating effective immunogens. Recent studies have identified the HIV-1 Env signal peptide (SP) as an important contributor to Env glycosylation. Further investigation into the mechanisms by which the SP directs glycosylation will be important, both in the context of understanding HIV-1 biology and in order to inform HIV-1 vaccine design.https://www.mdpi.com/2076-393X/9/2/176HIV-1HIV envelopeglycosylationsignal peptidePNGSbroadly neutralizing antibodies |
| spellingShingle | Gregory S. Lambert Chitra Upadhyay HIV-1 Envelope Glycosylation and the Signal Peptide Vaccines HIV-1 HIV envelope glycosylation signal peptide PNGS broadly neutralizing antibodies |
| title | HIV-1 Envelope Glycosylation and the Signal Peptide |
| title_full | HIV-1 Envelope Glycosylation and the Signal Peptide |
| title_fullStr | HIV-1 Envelope Glycosylation and the Signal Peptide |
| title_full_unstemmed | HIV-1 Envelope Glycosylation and the Signal Peptide |
| title_short | HIV-1 Envelope Glycosylation and the Signal Peptide |
| title_sort | hiv 1 envelope glycosylation and the signal peptide |
| topic | HIV-1 HIV envelope glycosylation signal peptide PNGS broadly neutralizing antibodies |
| url | https://www.mdpi.com/2076-393X/9/2/176 |
| work_keys_str_mv | AT gregoryslambert hiv1envelopeglycosylationandthesignalpeptide AT chitraupadhyay hiv1envelopeglycosylationandthesignalpeptide |