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HIV-1 protease |
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Vaxjo ID |
367 |
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Vaccine Adjuvant Name |
HIV-1 protease |
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Adjuvant VO ID |
VO_0005546
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Description |
genetic adjuvant that induces Th1 response |
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Stage of Development |
Research |
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Host Species for Testing |
Mouse |
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Components |
HIV protease (PR): mediates the processing of human immunodeficiency virus (HIV) polyproteins and is necessary for the viral production |
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Structure |
HIV PR consists of three domains: terminal, core, and flap domains, and each has a unique role in the proteolytic process (21). The substrate-binding site is found in the core domain that contains the catalytic triad (DTG). The terminal domain is required for dimerization, which is also important for its proteolytic activity, and the flap domain regulates substrate access |
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Preparation |
The wild-type HIV-1 PR gene (PR) was also codon optimized and synthesized by reverse translation. The catalytically attenuated PR (PRT26S) and inactivated PR (PRD25A) were constructed using the site-directed mutagenesis that replaced Thr-26 with Ser or Asp-25 with Ala, respectively. PRM46I and PRD25A/M46I were constructed in a similar manner. To generate HIV PR1-95, the HIV PR 1-95 region was PCR amplified and subcloned into pGX10. Mutations were verified by sequencing. |
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Function |
enhancing T-cell immune response via chaperonelike activity |
| References |
Kim et al., 2010: Kim KS, Jin DB, Ahn SS, Park KS, Seo SH, Suh YS, Sung YC. HIV-1 protease has a genetic T-cell adjuvant effect which is negatively regulated by proteolytic activity. Journal of virology. 2010; 84(15); 7743-7749. [PubMed: 20484507].
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