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Analysis and characterization of hepatitis B vaccine particles synthesized from Hansenula polymorpha
- Authors
- Seo, Hyuk-Seong; Park, Jin-Seung; Han, Kyung-Yeon; Bae, Kyung-Dong; Ahn, Sang Jeorn; Kang, Hyun Ah; Lee, Jeewon
- Issue Date
- 5-8월-2008
- Publisher
- ELSEVIER SCI LTD
- Keywords
- hepatitis B surface antigen; yeast; covalent multimer; glycosylation; stability
- Citation
- VACCINE, v.26, no.33, pp.4138 - 4144
- Indexed
- SCIE
SCOPUS
- Journal Title
- VACCINE
- Volume
- 26
- Number
- 33
- Start Page
- 4138
- End Page
- 4144
- ISSN
- 0264-410X
- 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. (C) 2008 Elsevier Ltd. All rights reserved,
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