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Protection of mice against pandemic H1N1 influenza virus challenge after immunization with baculovirus-expressed stabilizing peptide fusion hemagglutinin protein

 Eunji Yang  ;  Yonggeun Cho  ;  Jungah Choi  ;  Young Joo Choi  ;  Pil Gu Park  ;  Eunsun Park  ;  Choong Hwan Lee  ;  Hyeja Lee  ;  Jongsun Kim  ;  Jae Myun Lee  ;  Manki Song 
 Journal of Microbiology and Biotechnology, Vol.25(2) : 280-287, 2015 
Journal Title
 Journal of Microbiology and Biotechnology 
Issue Date
Animals ; Antibodies, Neutralizing/blood ; Antibodies, Neutralizing/immunology ; Antibodies, Viral/blood ; Antibodies, Viral/immunology* ; Baculoviridae/genetics* ; Disease Models, Animal ; Hemagglutinin Glycoproteins, Influenza Virus/genetics ; Hemagglutinin Glycoproteins, Influenza Virus/immunology* ; Humans ; Immunity, Humoral ; Influenza A Virus, H1N1 Subtype/immunology* ; Influenza Vaccines/immunology* ; Mice ; Mice, Inbred BALB C ; Orthomyxoviridae Infections/prevention & control* ; Recombinant Fusion Proteins/immunology ; Synucleins/genetics ; Vaccination ; Vaccines, Subunit/immunology
Pandemic ; influenza ; hemagglutinin ; stabilizing peptide
Current influenza vaccines are produced in embryonated chicken eggs. However, egg-based vaccines have various problems. To address these problems, recombinant protein vaccines have been developed as new vaccine candidates. Unfortunately, recombinant proteins frequently encounter aggregation and low stability during their biogenesis. It has been previously demonstrated that recombinantly expressed proteins can be greatly stabilized with high solubility by fusing stabilizing peptide (SP) derived from the C-terminal acidic tail of human synuclein (ATS). To investigate whether SP fusion proteins can induce protective immunity in mice, we produced influenza HA and SP fusion protein using a baculovirus expression system. In in vitro tests, SP-fused recombinant HA1 (SP-rHA1) was shown to be more stable than recombinant HA1 (rHA1). Mice were immunized intramuscularly with baculovirus-expressed rHA1 protein or SP-rHA1 protein ($2{\mu}g/mouse$ 수식 이미지) formulated with aluminum hydroxide. Antibody responses were determined by ELISA and hemagglutination inhibition assay. We observed that SP-rHA1 immunization elicited HA-specific antibody responses that were comparable to rHA1 immunization. These results indicate that fusion of SP to rHA1 does not negatively affect the immunogenicity of the vaccine candidate. Therefore, it is possible to apply SP fusion technology to develop stable recombinant protein vaccines with high solubility.
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1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Jong Sun(김종선) ORCID logo https://orcid.org/0000-0002-3149-669X
Park, Pil Gu(박필구) ORCID logo https://orcid.org/0000-0002-3024-3439
Lee, Jae Myun(이재면) ORCID logo https://orcid.org/0000-0002-5273-3113
Cho, Yonggeun(조용근) ORCID logo https://orcid.org/0000-0003-1946-4318
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