tetano
Editor, Senior Moderator
Nanomedicine
. 2022 Jan 29;102527.
doi: 10.1016/j.nano.2022.102527. Online ahead of print.
Recombinant VLPs empower RBM peptides showing no immunogenicity in native SARS-COV-2 protein to elicit a robust neutralizing antibody response
Qiong Long[SUP] 1 [/SUP], Ying Yang[SUP] 1 [/SUP], Mengli Yang[SUP] 2 [/SUP], Hongmei Bai[SUP] 1 [/SUP], Wengjia Sun[SUP] 1 [/SUP], Xu Yang[SUP] 1 [/SUP], Weiwei Huang[SUP] 1 [/SUP], Duo Li[SUP] 3 [/SUP], Yanbing Ma[SUP] 4 [/SUP]
Affiliations
Abstract
New SARS-COV-2 vaccine strategies are still urgently needed, especially for emerging virus mutations and variants. In this study, we focused on analyzing the antigenicity and vaccine potency of linear peptide epitopes located in receptor binding motif (RBM) of spike (S) protein. Nine 12 to 16-mer overlapping peptides (P1-P9) were synthesized chemically and coupled to carrier protein KLH for the immunization in mice. Four of identified peptides were further engineered to present on the surface of recombinant Hepatitis B core antigen (HBcAg) virus-like particles (VLPs) respectively. Antisera obtained from VLPs -immunized mice demonstrated strong reactivity and affinity to S1 protein or inactivated virus and neutralizing activity against virus infection in vitro. This study indicates that recombinant VLPs empower peptides which display underprivileged antigenicity in native protein to elicit high levels of neutralizing antibody, providing potential epitope candidates and an effective delivery strategy for the development of a multi-epitope vaccine.
Keywords: Epitope; Receptor-binding motif (RBM); Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2); Vaccine; Virus-like particles (VLPs).
. 2022 Jan 29;102527.
doi: 10.1016/j.nano.2022.102527. Online ahead of print.
Recombinant VLPs empower RBM peptides showing no immunogenicity in native SARS-COV-2 protein to elicit a robust neutralizing antibody response
Qiong Long[SUP] 1 [/SUP], Ying Yang[SUP] 1 [/SUP], Mengli Yang[SUP] 2 [/SUP], Hongmei Bai[SUP] 1 [/SUP], Wengjia Sun[SUP] 1 [/SUP], Xu Yang[SUP] 1 [/SUP], Weiwei Huang[SUP] 1 [/SUP], Duo Li[SUP] 3 [/SUP], Yanbing Ma[SUP] 4 [/SUP]
Affiliations
- PMID: 35104670
- DOI: 10.1016/j.nano.2022.102527
Abstract
New SARS-COV-2 vaccine strategies are still urgently needed, especially for emerging virus mutations and variants. In this study, we focused on analyzing the antigenicity and vaccine potency of linear peptide epitopes located in receptor binding motif (RBM) of spike (S) protein. Nine 12 to 16-mer overlapping peptides (P1-P9) were synthesized chemically and coupled to carrier protein KLH for the immunization in mice. Four of identified peptides were further engineered to present on the surface of recombinant Hepatitis B core antigen (HBcAg) virus-like particles (VLPs) respectively. Antisera obtained from VLPs -immunized mice demonstrated strong reactivity and affinity to S1 protein or inactivated virus and neutralizing activity against virus infection in vitro. This study indicates that recombinant VLPs empower peptides which display underprivileged antigenicity in native protein to elicit high levels of neutralizing antibody, providing potential epitope candidates and an effective delivery strategy for the development of a multi-epitope vaccine.
Keywords: Epitope; Receptor-binding motif (RBM); Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2); Vaccine; Virus-like particles (VLPs).