Design and Preliminary Immunogenicity Evaluation of Nipah Virus Glycoprotein G Epitope-Based Peptide Vaccine in Mice
Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Methods: Herein, NiV...
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| Published in | Vaccines (Basel) Vol. 13; no. 4; p. 428 |
|---|---|
| Main Authors | , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Switzerland
MDPI AG
18.04.2025
MDPI |
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| Online Access | Get full text |
| ISSN | 2076-393X 2076-393X |
| DOI | 10.3390/vaccines13040428 |
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| Abstract | Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Methods: Herein, NiV attachment glycoprotein G (NiV-G), which is crucial to host cell receptor binding, was used to develop Nipah epitope-based peptide vaccines. A total of 39 B- and T-cell epitopes of NiV-G were shortlisted for peptide synthesis and evaluation using in silico analysis. Results: The in vitro antigenicity evaluation of the peptide candidates showed eight synthesized peptides (G7, stalk-domain epitopes) with relatively high binding to NiV-G antibody-positive serum (A450nm: 1.39–3.78). Moreover, nine-mer (9-mer) peptides were found to be less reactive than their longer peptide counterparts (15–30 aa, G7-1, and G7-4), but 9-mer activity was enhanced with cyclization (NPLPFREYK, A450nm: 2.66) and C-terminal amidation modification (NPLPFREYK-NH2, A450nm: 1.39). Subsequently, in vivo validation in immunized mice revealed the immunogenicity potential of the G7-1 peptide vaccine (30 aa, NENVNEKCKFTLPPLKIHECNISCPNPLPF) to elicit a strong antigen-specific antibody response against their homologous peptide antigen (I.V., A450nm: 1.48 ± 0.78; I.M., A450nm: 1.66 ± 0.66). However, antibody binding to recombinant NiV-G protein remained low, suggesting limited recognition to the native antigen. Conclusions: This study focused on the preliminary screening and validation of peptide vaccines using single formulations with minimal modifications in the peptide candidates. Our findings collectively show the immunogenic potential of the NiV-G stalk-based epitope peptide vaccine as a novel therapeutic for NiV and underscores the need for strategic design, delivery, and formulation optimization to enhance its protective efficacy and translational application. |
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| AbstractList | Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Methods: Herein, NiV attachment glycoprotein G (NiV-G), which is crucial to host cell receptor binding, was used to develop Nipah epitope-based peptide vaccines. A total of 39 B- and T-cell epitopes of NiV-G were shortlisted for peptide synthesis and evaluation using in silico analysis. Results: The in vitro antigenicity evaluation of the peptide candidates showed eight synthesized peptides (G7, stalk-domain epitopes) with relatively high binding to NiV-G antibody-positive serum (A[sub.450nm] : 1.39–3.78). Moreover, nine-mer (9-mer) peptides were found to be less reactive than their longer peptide counterparts (15–30 aa, G7-1, and G7-4), but 9-mer activity was enhanced with cyclization (NPLPFREYK, A[sub.450nm] : 2.66) and C-terminal amidation modification (NPLPFREYK-NH2, A[sub.450nm] : 1.39). Subsequently, in vivo validation in immunized mice revealed the immunogenicity potential of the G7-1 peptide vaccine (30 aa, NENVNEKCKFTLPPLKIHECNISCPNPLPF) to elicit a strong antigen-specific antibody response against their homologous peptide antigen (I.V., A[sub.450nm] : 1.48 ± 0.78; I.M., A[sub.450nm] : 1.66 ± 0.66). However, antibody binding to recombinant NiV-G protein remained low, suggesting limited recognition to the native antigen. Conclusions: This study focused on the preliminary screening and validation of peptide vaccines using single formulations with minimal modifications in the peptide candidates. Our findings collectively show the immunogenic potential of the NiV-G stalk-based epitope peptide vaccine as a novel therapeutic for NiV and underscores the need for strategic design, delivery, and formulation optimization to enhance its protective efficacy and translational application. Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Methods: Herein, NiV attachment glycoprotein G (NiV-G), which is crucial to host cell receptor binding, was used to develop Nipah epitope-based peptide vaccines. A total of 39 B- and T-cell epitopes of NiV-G were shortlisted for peptide synthesis and evaluation using in silico analysis. Results: The in vitro antigenicity evaluation of the peptide candidates showed eight synthesized peptides (G7, stalk-domain epitopes) with relatively high binding to NiV-G antibody-positive serum (A 450nm : 1.39–3.78). Moreover, nine-mer (9-mer) peptides were found to be less reactive than their longer peptide counterparts (15–30 aa, G7-1, and G7-4), but 9-mer activity was enhanced with cyclization (NPLPFREYK, A 450nm : 2.66) and C-terminal amidation modification (NPLPFREYK-NH2, A 450nm : 1.39). Subsequently, in vivo validation in immunized mice revealed the immunogenicity potential of the G7-1 peptide vaccine (30 aa, NENVNEKCKFTLPPLKIHECNISCPNPLPF) to elicit a strong antigen-specific antibody response against their homologous peptide antigen (I.V., A 450nm : 1.48 ± 0.78; I.M., A 450nm : 1.66 ± 0.66). However, antibody binding to recombinant NiV-G protein remained low, suggesting limited recognition to the native antigen. Conclusions: This study focused on the preliminary screening and validation of peptide vaccines using single formulations with minimal modifications in the peptide candidates. Our findings collectively show the immunogenic potential of the NiV-G stalk-based epitope peptide vaccine as a novel therapeutic for NiV and underscores the need for strategic design, delivery, and formulation optimization to enhance its protective efficacy and translational application. Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Methods: Herein, NiV attachment glycoprotein G (NiV-G), which is crucial to host cell receptor binding, was used to develop Nipah epitope-based peptide vaccines. A total of 39 B- and T-cell epitopes of NiV-G were shortlisted for peptide synthesis and evaluation using in silico analysis. Results: The in vitro antigenicity evaluation of the peptide candidates showed eight synthesized peptides (G7, stalk-domain epitopes) with relatively high binding to NiV-G antibody-positive serum (A450nm: 1.39–3.78). Moreover, nine-mer (9-mer) peptides were found to be less reactive than their longer peptide counterparts (15–30 aa, G7-1, and G7-4), but 9-mer activity was enhanced with cyclization (NPLPFREYK, A450nm: 2.66) and C-terminal amidation modification (NPLPFREYK-NH2, A450nm: 1.39). Subsequently, in vivo validation in immunized mice revealed the immunogenicity potential of the G7-1 peptide vaccine (30 aa, NENVNEKCKFTLPPLKIHECNISCPNPLPF) to elicit a strong antigen-specific antibody response against their homologous peptide antigen (I.V., A450nm: 1.48 ± 0.78; I.M., A450nm: 1.66 ± 0.66). However, antibody binding to recombinant NiV-G protein remained low, suggesting limited recognition to the native antigen. Conclusions: This study focused on the preliminary screening and validation of peptide vaccines using single formulations with minimal modifications in the peptide candidates. Our findings collectively show the immunogenic potential of the NiV-G stalk-based epitope peptide vaccine as a novel therapeutic for NiV and underscores the need for strategic design, delivery, and formulation optimization to enhance its protective efficacy and translational application. The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Herein, NiV attachment glycoprotein G (NiV-G), which is crucial to host cell receptor binding, was used to develop Nipah epitope-based peptide vaccines. A total of 39 B- and T-cell epitopes of NiV-G were shortlisted for peptide synthesis and evaluation using in silico analysis. The in vitro antigenicity evaluation of the peptide candidates showed eight synthesized peptides (G7, stalk-domain epitopes) with relatively high binding to NiV-G antibody-positive serum (A : 1.39-3.78). Moreover, nine-mer (9-mer) peptides were found to be less reactive than their longer peptide counterparts (15-30 aa, G7-1, and G7-4), but 9-mer activity was enhanced with cyclization (NPLPFREYK, A : 2.66) and C-terminal amidation modification (NPLPFREYK-NH2, A : 1.39). Subsequently, in vivo validation in immunized mice revealed the immunogenicity potential of the G7-1 peptide vaccine (30 aa, NENVNEKCKFTLPPLKIHECNISCPNPLPF) to elicit a strong antigen-specific antibody response against their homologous peptide antigen (I.V., A : 1.48 ± 0.78; I.M., A : 1.66 ± 0.66). However, antibody binding to recombinant NiV-G protein remained low, suggesting limited recognition to the native antigen. This study focused on the preliminary screening and validation of peptide vaccines using single formulations with minimal modifications in the peptide candidates. Our findings collectively show the immunogenic potential of the NiV-G stalk-based epitope peptide vaccine as a novel therapeutic for NiV and underscores the need for strategic design, delivery, and formulation optimization to enhance its protective efficacy and translational application. Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Methods: Herein, NiV attachment glycoprotein G (NiV-G), which is crucial to host cell receptor binding, was used to develop Nipah epitope-based peptide vaccines. A total of 39 B- and T-cell epitopes of NiV-G were shortlisted for peptide synthesis and evaluation using in silico analysis. Results: The in vitro antigenicity evaluation of the peptide candidates showed eight synthesized peptides (G7, stalk-domain epitopes) with relatively high binding to NiV-G antibody-positive serum (A450nm: 1.39-3.78). Moreover, nine-mer (9-mer) peptides were found to be less reactive than their longer peptide counterparts (15-30 aa, G7-1, and G7-4), but 9-mer activity was enhanced with cyclization (NPLPFREYK, A450nm: 2.66) and C-terminal amidation modification (NPLPFREYK-NH2, A450nm: 1.39). Subsequently, in vivo validation in immunized mice revealed the immunogenicity potential of the G7-1 peptide vaccine (30 aa, NENVNEKCKFTLPPLKIHECNISCPNPLPF) to elicit a strong antigen-specific antibody response against their homologous peptide antigen (I.V., A450nm: 1.48 ± 0.78; I.M., A450nm: 1.66 ± 0.66). However, antibody binding to recombinant NiV-G protein remained low, suggesting limited recognition to the native antigen. Conclusions: This study focused on the preliminary screening and validation of peptide vaccines using single formulations with minimal modifications in the peptide candidates. Our findings collectively show the immunogenic potential of the NiV-G stalk-based epitope peptide vaccine as a novel therapeutic for NiV and underscores the need for strategic design, delivery, and formulation optimization to enhance its protective efficacy and translational application.Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts necessary. Although NiV is a zoonotic pathogen with high case fatality, there is still no licensed vaccine. Methods: Herein, NiV attachment glycoprotein G (NiV-G), which is crucial to host cell receptor binding, was used to develop Nipah epitope-based peptide vaccines. A total of 39 B- and T-cell epitopes of NiV-G were shortlisted for peptide synthesis and evaluation using in silico analysis. Results: The in vitro antigenicity evaluation of the peptide candidates showed eight synthesized peptides (G7, stalk-domain epitopes) with relatively high binding to NiV-G antibody-positive serum (A450nm: 1.39-3.78). Moreover, nine-mer (9-mer) peptides were found to be less reactive than their longer peptide counterparts (15-30 aa, G7-1, and G7-4), but 9-mer activity was enhanced with cyclization (NPLPFREYK, A450nm: 2.66) and C-terminal amidation modification (NPLPFREYK-NH2, A450nm: 1.39). Subsequently, in vivo validation in immunized mice revealed the immunogenicity potential of the G7-1 peptide vaccine (30 aa, NENVNEKCKFTLPPLKIHECNISCPNPLPF) to elicit a strong antigen-specific antibody response against their homologous peptide antigen (I.V., A450nm: 1.48 ± 0.78; I.M., A450nm: 1.66 ± 0.66). However, antibody binding to recombinant NiV-G protein remained low, suggesting limited recognition to the native antigen. Conclusions: This study focused on the preliminary screening and validation of peptide vaccines using single formulations with minimal modifications in the peptide candidates. Our findings collectively show the immunogenic potential of the NiV-G stalk-based epitope peptide vaccine as a novel therapeutic for NiV and underscores the need for strategic design, delivery, and formulation optimization to enhance its protective efficacy and translational application. |
| Audience | Academic |
| Author | Kim, Woo H. Lim, Heeji Ouh, In-Ohk Lee, Seung Yun Altanzul, Bujinlkham Kim, Seungyeon Jang, Eun Young Flores, Rochelle A. Lee, Yoo-kyoung Baek, Jiwon Choi, Eun Bee Moon, Seo Young |
| AuthorAffiliation | 1 Division of Vaccine Development Coordination, Center for Vaccine Research, National Institute of Infectious Diseases, National Institute of Health, Korea Disease Control and Prevention Agency, Osong, Cheongju 28159, Chungcheongbuk-do, Republic of Korea; hatmddus135@korea.kr (S.K.); msy1477@korea.kr (S.Y.M.); jiwonbb@korea.kr (J.B.); dmsql2274@korea.kr (E.B.C.); dalgi0519@korea.kr (H.L.); sky11kk@korea.kr (E.Y.J.); leeykyoung@korea.kr (Y.-k.L.) 2 College of Veterinary Medicine & Institute of Animal Medicine, Gyeongsang National University, Jinju 52828, Gyeongsangnam-do, Republic of Korea; floresrochellea@gmail.com (R.A.F.); seungyun0218@gnu.ac.kr (S.Y.L.); bujinlkham_1221@gnu.ac.kr (B.A.) |
| AuthorAffiliation_xml | – name: 1 Division of Vaccine Development Coordination, Center for Vaccine Research, National Institute of Infectious Diseases, National Institute of Health, Korea Disease Control and Prevention Agency, Osong, Cheongju 28159, Chungcheongbuk-do, Republic of Korea; hatmddus135@korea.kr (S.K.); msy1477@korea.kr (S.Y.M.); jiwonbb@korea.kr (J.B.); dmsql2274@korea.kr (E.B.C.); dalgi0519@korea.kr (H.L.); sky11kk@korea.kr (E.Y.J.); leeykyoung@korea.kr (Y.-k.L.) – name: 2 College of Veterinary Medicine & Institute of Animal Medicine, Gyeongsang National University, Jinju 52828, Gyeongsangnam-do, Republic of Korea; floresrochellea@gmail.com (R.A.F.); seungyun0218@gnu.ac.kr (S.Y.L.); bujinlkham_1221@gnu.ac.kr (B.A.) |
| Author_xml | – sequence: 1 givenname: Seungyeon surname: Kim fullname: Kim, Seungyeon – sequence: 2 givenname: Rochelle A. orcidid: 0000-0002-8848-6652 surname: Flores fullname: Flores, Rochelle A. – sequence: 3 givenname: Seo Young surname: Moon fullname: Moon, Seo Young – sequence: 4 givenname: Seung Yun surname: Lee fullname: Lee, Seung Yun – sequence: 5 givenname: Bujinlkham surname: Altanzul fullname: Altanzul, Bujinlkham – sequence: 6 givenname: Jiwon surname: Baek fullname: Baek, Jiwon – sequence: 7 givenname: Eun Bee surname: Choi fullname: Choi, Eun Bee – sequence: 8 givenname: Heeji orcidid: 0000-0003-3546-9477 surname: Lim fullname: Lim, Heeji – sequence: 9 givenname: Eun Young surname: Jang fullname: Jang, Eun Young – sequence: 10 givenname: Yoo-kyoung surname: Lee fullname: Lee, Yoo-kyoung – sequence: 11 givenname: In-Ohk surname: Ouh fullname: Ouh, In-Ohk – sequence: 12 givenname: Woo H. orcidid: 0000-0002-6874-6787 surname: Kim fullname: Kim, Woo H. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/40333318$$D View this record in MEDLINE/PubMed |
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| Keywords | epitopes vaccine Nipah virus peptide vaccine attachment glycoprotein G |
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| Snippet | Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic... The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic preparedness efforts... Background: The emergence of several paramyxoviruses, including Nipah virus (NiV), makes continued efforts in vaccine development as part of pandemic... |
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| SubjectTerms | Amino acids Antibodies Antibody response Antigenic determinants Antigenicity Antigens attachment glycoprotein G Binding Carbohydrates Clinical trials Dengue fever Design optimization Epidemics Epitopes Genomes Glycoprotein G Glycoproteins Immunity (Disease) Immunization Immunogenicity Infections Infectious diseases Lymphocytes T Monoclonal antibodies Nipah virus Pandemics Pathogens Peptide synthesis peptide vaccine Peptides Pharmaceutical research Proteins R&D Research & development vaccine Vaccine development Vaccines Viral proteins Viral vaccines Viruses Zoonoses |
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| Title | Design and Preliminary Immunogenicity Evaluation of Nipah Virus Glycoprotein G Epitope-Based Peptide Vaccine in Mice |
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