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

作者：Seo Hyuk Seong; Park Jin Seung; Han Kyung Yeon; Bae Kyung Dong; Ahn Sang Jeorn; Kang Hyun Ah; Lee Jeewon^*

来源：Vaccine, 2008, 26(33): 4138-4144.

DOI：10.1016/j.vaccine.2008.05.070

• hepatitis B surface antigen
• yeast
• covalent multimer
• glycosylation
• stability

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.

• 出版日期2008-8-5