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Koo, Hyun Na;Bae, Sung Min;Woo, Soo Dong
- International Journal of Industrial Entomology and Biomaterials
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- v.32 no.2
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- pp.90-97
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- 2016
The major structural proteins of porcine reproductive and respiratory syndrome virus (PRRSV) are derived from ORFs 4, 5, and 6. They have been considered very important to arouse the humoral and cellular immune responses against PRRSV infection and proposed to be the excellent candidate proteins in the design of PRRS bioengineering vaccine. However, the PRRSV structural proteins are produced in low levels in the infected cells because it forms insoluble protein and possesses several transmembrane regions. To overcome this problem, we fused the ORF4, ORF5, and ORF6 with SUMO (small ubiquitin-related modifier). The resulting fusion protein SUMO-ORF4, -ORF5, and -ORF6 were highly expressed in Bm5 cells. The level of protein expression using the Bombyx mori larvae was higher than that using Bm5 cells. In addition, fusion to SUMOstar, which is not processed by native SUMO proteases, significantly enhanced protein expression levels compared to SUMO fusion. This study demonstrated that SUMO or SUMOstar, when fused with PRRSV structural proteins, was able to promote its soluble expression. This may be a better method to produce PRRSV structural proteins for vaccine development.
https://doi.org/10.7852/ijie.2016.32.2.90 인용 PDF KSCI KPUBS

Rhim, Jae-Hwan;Yesun Han;Kim, Sung-Hou;Yunje Cho
- Proceedings of the Korean Biophysical Society Conference
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- 1996.07a
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- pp.30-30
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- 1996
A suproxide dismutase gene of Aquifex pyroprolus, a novel marine hypenhermophilic bacterium, was cloned, expressed, and characterized. The SOD of A pyrophilus (ApSOD) is an iron-containing homo-oligomeric protein with a monomeric molecular weight of 24.2 kDa. the amino acid sequence is similar to those of known Mn- and Fe-SODs from thermophilic archaea, and metal binding residues in all SOD sequences from different species are also conserved in A. pyrophilus SOD. (omitted)
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Jung, Jin-Won;Lee, Weon-Tae
- BMB Reports
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- v.37 no.1
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- pp.28-34
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- 2004
The discovery of biochemical and cellular functions of unannotated gene products begins with a database search of proteins with structure/sequence homologues based on known genes. Very recently, a number of frontier groups in structural biology proposed a new paradigm to predict biological functions of an unknown protein on the basis of its three-dimensional structure on a genomic scale. Structural proteomics (genomics), a research area for structure-based functional discovery, aims to complete the protein-folding universe of all gene products in a cell. It would lead us to a complete understanding of a living organism from protein structure. Two major complementary experimental techniques, X-ray crystallography and NMR spectroscopy, combined with recently developed high throughput methods have played a central role in structural proteomics research; however, an integration of these methodologies together with comparative modeling and electron microscopy would speed up the goal for completing a full dictionary of protein folding space in the near future.
https://doi.org/10.5483/BMBRep.2004.37.1.028 인용 PDF

Choe, Rim-Soon;Shin, Kil-Sang;Joo, Chung-No;Hwang, Dae-Yeon
- Applied Microscopy
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- v.18 no.1
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- pp.77-91
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- 1988
Since the Urechis unicinctus-oocyte grows asynchronously in the body fluid, various oocytes in developmental stages can be prepared from each individual. The oocytes obtained from the coelomic fluid are then classified into five developmental stages according to the fine structural features. The earlier oocytes (${\sim}18{\mu}m$) form cluster and thereafter the oocytes grow singly without a distinct support of somatic cell, such as accessory cell or matrix cell. The yolk granules begin to appear already in the oocyte of cluster stage, however, the typical yolk was observed at the stage IV. Therefore, it was suggested that the yolk deposition is correlated with the coelomic fluid. The mature oocyte measured about $150{\mu}m$ produces the invagination not only on oolemma(indentation) but also on nuclear envelope. After the formation of the indentation, the mature ooytes are stored in storge sacs. The fine structural features were combined in aspect of structural concept of light microscopical observation.
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