Vasostatin has previously been expressed in fused form or in inclusion body form in Escherichia coli. Here the protein was expressed in soluble non-fusion form in BL21(DE3)pLysS by IPTG induction. The expression level of vasostatin was about 15% of the total cellular protein. The expressed vasostatin was purified and its biological activity was investigated by an endothelial cell proliferation assay.
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http://dx.doi.org/10.2174/0929866054696163 | DOI Listing |
NPJ Vaccines
October 2022
State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Life Sciences, School of Public Health, Xiamen University, Xiamen, 361102, China.
In vaccinology, a potent immunogen has two prerequisite attributes-antigenicity and immunogenicity. We have rational designed a triple-type HPV vaccine against HPV58, -33 and -52 covered in Gardasil 9 based on the sequence homology and similar surface loop structure of L1 protein, which is related to cross-type antigenicity. Here, we design another triple-type vaccine against non-vaccine types HPV39, -68 and -70 by immunogenicity optimization considering type specific immunodominant epitopes located in separate region for different types.
View Article and Find Full Text PDFFront Bioeng Biotechnol
January 2020
Department of Integrative Biotechnology, College of Biotechnology and Bioengineering, Sungkyunkwan University, Suwon-si, South Korea.
Recombinant whole-cell biocatalysts are widely used for biotransformation of valuable products. However, some key enzymes involved in biotransformation processes are unstable and cannot be easily expressed in the functional form. In this study, we describe a versatile platform for enzyme stabilization inside the cell: Intracellularly Immobilized Enzyme System (IIES).
View Article and Find Full Text PDFMicrob Cell Fact
March 2018
Institute of Agro-food Science and Technology, Chinese Academy of Agricultural Sciences (CAAS), Beijing, 100193, China.
Background: Thermostable lipases from microbial sources have been substantially overexpressed in E. coli, however, these enzymes are often produced with low-level enzymatic activity and mainly in the form of inclusion bodies. Several studies have reported that the secretory production of recombinant proteins fused their N-terminus to a signal peptide has been employed to resolve the problem.
View Article and Find Full Text PDFVaccine
August 2017
National Institute of Diagnostics and Vaccine Development in Infectious Disease, School of Life Sciences, Xiamen University, Xiamen 361102, China; State Key Laboratory of Molecular Vaccinology and Molecular Diagnostics, School of Public Health, Xiamen University, Xiamen 361102, China. Electronic address:
Human papillomavirus (HPV) types 16 and 18 account for approximately 70% of cervical cancer worldwide. Neutralizing HPV prophylactic vaccines offer significant benefit, as they block HPV infection and prevent subsequent disease. However, the three licensed HPV vaccines that cover these two genotypes were produced in eukaryotic cells, which is expensive, particularly for low-income countries where HPV is highest.
View Article and Find Full Text PDFProtein J
April 2016
Heilongjiang Key Laboratory of Anti-fibrosis Biotherapy, Mudanjiang Medical University, Mudanjiang, 157011, People's Republic of China.
Ubiquitin-like protease 1 (Ulp1) of Saccharomyces cerevisiae emerges as a fundamental tool to obtain the natural N-terminal target protein by cleavage of the small ubiquitin-related modifier (SUMO) fusion protein. However, the costly commercial Ulp1 and its complicated procedures limit its application in the preparation of the target protein with natural N-terminal sequence. Here, we describe the preparation of bioactive codon-optimized recombinant truncated Ulp1 (Leu403-Lys621) (rtUlp1) of S.
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