Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha

Hyuk Seong Seo; Jin Seung Park; Kyung Yeon Han; Kyung Dong Bae; Sang Jeom Ahn; Hyun Ah Kang; Jeewon Lee

doi:10.1016/j.vaccine.2008.05.070

Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha

Hyuk Seong Seo, Jin Seung Park, Kyung Yeon Han, Kyung Dong Bae, Sang Jeom Ahn, Hyun Ah Kang, Jeewon Lee

Department of Chemical and Biological Engineering

Research output: Contribution to journal › Article › peer-review

19 Citations (Scopus)

Abstract

The biochemical and physical properties of hepatitis B virus (HBV) small surface antigen (S-HBVsAg) from Berna Biotech Korea Corp. were systematically analyzed and characterized. Through various electrophoresis and immunoblotting assay of S-HBVsAg and its proteolytic products, it was confirmed that the S-HBVsAg vaccine particles are present in the form of covalent multimers that are assembled via strong intermolecular disulfide bonds. The S-HBVsAg particles contain no N-glycosylation moiety but some O-glycosidically linked mannoses. Evidently from N-terminus sequencing of both monomers and dimers that are formed by complete and partial reduction, respectively, of the S-HBVsAg particles under reducing SDS-PAGE condition, it is evident that each polypeptide within S-HBVsAg particles has authentic sequence of N-terminus. Denaturation plot shows that the S-HBVsAg vaccine particles were extremely stable especially in the solution with high acidity. This stability property of S-HBVsAg vaccine particles could provide very useful information for the optimization of the downstream process of recombinant S-HBVsAg particles synthesized from yeast cultures.

Original language	English
Pages (from-to)	4138-4144
Number of pages	7
Journal	Vaccine
Volume	26
Issue number	33
DOIs	https://doi.org/10.1016/j.vaccine.2008.05.070
Publication status	Published - 2008 Aug 5

Keywords

Covalent multimer
Glycosylation
Hepatitis B surface antigen
Stability
Yeast

ASJC Scopus subject areas

Molecular Medicine
Immunology and Microbiology(all)
veterinary(all)
Public Health, Environmental and Occupational Health
Infectious Diseases

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1016/j.vaccine.2008.05.070

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title = "Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha",

abstract = "The biochemical and physical properties of hepatitis B virus (HBV) small surface antigen (S-HBVsAg) from Berna Biotech Korea Corp. were systematically analyzed and characterized. Through various electrophoresis and immunoblotting assay of S-HBVsAg and its proteolytic products, it was confirmed that the S-HBVsAg vaccine particles are present in the form of covalent multimers that are assembled via strong intermolecular disulfide bonds. The S-HBVsAg particles contain no N-glycosylation moiety but some O-glycosidically linked mannoses. Evidently from N-terminus sequencing of both monomers and dimers that are formed by complete and partial reduction, respectively, of the S-HBVsAg particles under reducing SDS-PAGE condition, it is evident that each polypeptide within S-HBVsAg particles has authentic sequence of N-terminus. Denaturation plot shows that the S-HBVsAg vaccine particles were extremely stable especially in the solution with high acidity. This stability property of S-HBVsAg vaccine particles could provide very useful information for the optimization of the downstream process of recombinant S-HBVsAg particles synthesized from yeast cultures.",

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author = "Seo, {Hyuk Seong} and Park, {Jin Seung} and Han, {Kyung Yeon} and Bae, {Kyung Dong} and Ahn, {Sang Jeom} and Kang, {Hyun Ah} and Jeewon Lee",

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T1 - Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha

AU - Seo, Hyuk Seong

AU - Park, Jin Seung

AU - Han, Kyung Yeon

AU - Bae, Kyung Dong

AU - Ahn, Sang Jeom

AU - Kang, Hyun Ah

AU - Lee, Jeewon

PY - 2008/8/5

Y1 - 2008/8/5

N2 - The biochemical and physical properties of hepatitis B virus (HBV) small surface antigen (S-HBVsAg) from Berna Biotech Korea Corp. were systematically analyzed and characterized. Through various electrophoresis and immunoblotting assay of S-HBVsAg and its proteolytic products, it was confirmed that the S-HBVsAg vaccine particles are present in the form of covalent multimers that are assembled via strong intermolecular disulfide bonds. The S-HBVsAg particles contain no N-glycosylation moiety but some O-glycosidically linked mannoses. Evidently from N-terminus sequencing of both monomers and dimers that are formed by complete and partial reduction, respectively, of the S-HBVsAg particles under reducing SDS-PAGE condition, it is evident that each polypeptide within S-HBVsAg particles has authentic sequence of N-terminus. Denaturation plot shows that the S-HBVsAg vaccine particles were extremely stable especially in the solution with high acidity. This stability property of S-HBVsAg vaccine particles could provide very useful information for the optimization of the downstream process of recombinant S-HBVsAg particles synthesized from yeast cultures.

AB - The biochemical and physical properties of hepatitis B virus (HBV) small surface antigen (S-HBVsAg) from Berna Biotech Korea Corp. were systematically analyzed and characterized. Through various electrophoresis and immunoblotting assay of S-HBVsAg and its proteolytic products, it was confirmed that the S-HBVsAg vaccine particles are present in the form of covalent multimers that are assembled via strong intermolecular disulfide bonds. The S-HBVsAg particles contain no N-glycosylation moiety but some O-glycosidically linked mannoses. Evidently from N-terminus sequencing of both monomers and dimers that are formed by complete and partial reduction, respectively, of the S-HBVsAg particles under reducing SDS-PAGE condition, it is evident that each polypeptide within S-HBVsAg particles has authentic sequence of N-terminus. Denaturation plot shows that the S-HBVsAg vaccine particles were extremely stable especially in the solution with high acidity. This stability property of S-HBVsAg vaccine particles could provide very useful information for the optimization of the downstream process of recombinant S-HBVsAg particles synthesized from yeast cultures.

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KW - Glycosylation

KW - Hepatitis B surface antigen

KW - Stability

KW - Yeast

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Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha

Abstract

Keywords

ASJC Scopus subject areas

UN SDGs

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