Production and product quality assessment of human hepatitis B virus pre-S2 antigen in submerged and solid-state cultures of Aspergillus oryzae

• Published in: Journal of bioscience and bioengineering Vol. 90; no. 1; pp. 118 - 120
• Main Authors: Maruyama, Jun-Ichi, Ohnuma, Hitoshi, Yoshikawa, Akira, Kadokura, Hiroshi, Nakajima, Harushi, Kitamoto, Katsuhiko
• Format: Journal Article
• Language: English
• Published: Amsterdarm Elsevier B.V 2000; Elsevier Science
• Subjects: ANTIGENS; ASPERGILLUS ORYZAE; Biological and medical sciences; Biotechnology; CULTURE TECHNIQUES; Fundamental and applied biological sciences. Psychology; Fungi; glaA gene; Health. Pharmaceutical industry; HEPATITIS; Hepatitis B virus; human hepatitis B virus; Industrial applications and implications. Economical aspects; Plant cell culture; pre-S protein; pre-S2; pre-S2 gene; Production of active biomolecules; Proteins; solid-state culture; submerged culture; Vaccins; VIRUSES; submerged culture; human hepatitis B virus; pre-S2; Aspergillus oryzae; solid-state culture; Human; Industrial application; Orthohepadnavirus; Glycosylation; Vaccine; Fungi; Virus; Submerged culture; Hepadnaviridae; Production; Microorganism culture; Solid substrate fermentation; Fungi Imperfecti; Hepatitis B virus; Pharmaceutical industry; Thallophyta
• ISSN: 1389-1723; 1347-4421
• DOI: 10.1016/S1389-1723(00)80045-6

Pre-S2 is a diagnostically important antigen of human hepatitis B virus (HBV). In order to produce pre-S2 antigen in Aspergillus oryzae, the gene [ pre-S2] 3, which encodes a tandemly triplicated repeat of pre-S2 polypeptides was fused with the partial glaA gene encoding glucoamylase lacking the starch-binding domain. In submerged culture, A. oryzae transformants carrying glaA-[ pre-S2] 3 secreted a heterogeneously glycosylated form of the fusion protein that was partially degraded. Contrarily, utilization of a wheat brain solid-state culture system resulted in the secretion of a homogeneous glycosylated form of the whole fusion protein. This is the first report of a dissimilarity in glycosylated modification between submerged and solid-state culture conditions in heterologous protein production in A. oryzae.