1. A truncated fragment of Ov-ASP-1 consisting of the core pathogenesis-related-1 (PR-1) domain maintains adjuvanticity as the full-length protein
- Author
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Lanying Du, Weilai Sun, Yusen Zhou, Jingjing Guo, Sara Lustigman, Wenjun Xiao, Yi Yang, Hong Yu, Shibo Jiang, and Zhihua Kou
- Subjects
Helminth protein ,Peptide ,law.invention ,CAP, CRISPS, Ag 5 and PR-1 ,Mice ,law ,Pathogenesis-related-1 family ,Adjuvant ,chemistry.chemical_classification ,Immunity, Cellular ,ASPPR, PR-1 domain of Ov-ASP-1 ,biology ,Helminth Proteins ,Infectious Diseases ,Recombinant DNA ,Molecular Medicine ,Female ,Protein family ,Ovalbumin ,Antibodies, Helminth ,CRISPS, cysteine-rich secretory protein ,Article ,OVA, ovalbumin ,Interferon-gamma ,FBS, fetal bovine serum ,Th1/Th2 immune responses ,Adjuvants, Immunologic ,Antigen ,Adjuvanticity ,parasitic diseases ,Ov-ASP-1 ,Animals ,Humans ,Protein Interaction Domains and Motifs ,Hepatitis B Antibodies ,Hepatitis B Surface Antigens ,General Veterinary ,General Immunology and Microbiology ,Public Health, Environmental and Occupational Health ,Ov-ASP-1, Onchocerca volvulus activation-associated secreted protein-1 ,PR-1, pathogenesis-related 1 ,Fusion protein ,Virology ,Molecular biology ,Immunity, Humoral ,Onchocerca volvulus ,chemistry ,HIV-1 ,biology.protein ,Immunization ,Ag 5, antigen 5 ,Interleukin-4 ,HBsAg, Hepatitis B virus surface antigen - Abstract
Highlights • Ov-ASP-1, an onchocerca volvulus protein, has good adjuvanticity for protein antigens. • A truncated Ov-ASP-1 (ASPPR) maintains adjuvanticity as the full-length of Ov-ASP-1. • ASPPR augments humoral and cellular immune responses elicited by protein antigens. • ASPPR has potential to be further developed as a novel adjuvant for human use., The Onchocerca volvulus activation-associated secreted protein-1 (Ov-ASP-1) has good adjuvanticity for a variety of antigens and vaccines, probably due to its ability activate antigen-processing cells (APCs). However, the functional domain of Ov-ASP-1 as an adjuvant is not clearly defined. Based on the structural prediction of this protein family, we constructed a 16-kDa recombinant protein of Ov-ASP-1 that contains only the core pathogenesis-related-1 (PR-1) domain (residues 10–153), designated ASPPR. We found that ASPPR exhibits adjuvanticity similar to that of the full-length Ov-ASP-1 (residues 10–220) for various antigens, including ovalbumin (OVA), HBsAg protein antigen, and the HIV peptide 5 (Pep5) antigen, but it is more suitable for vaccine design in ASPPR-antigen fusion proteins, and more stable in PBS than Ov-ASP-1 stored at −70 °C. These results suggest that ASPPR might be the functional region of Ov-ASP-1 as an adjuvant, and therefore could be developed as an adjuvant for human use.
- Published
- 2015