scholarly journals CTLA4Fcε, a novel soluble fusion protein that binds B7 molecules and the IgE receptors, and reduces humanin vitrosoluble CD23 production and lymphocyte proliferation

Immunology ◽  
2016 ◽  
Vol 148 (1) ◽  
pp. 40-55 ◽  
Author(s):  
Daniel Perez-Witzke ◽  
María Auxiliadora Miranda-García ◽  
Nuris Suárez ◽  
Raquel Becerra ◽  
Kharelys Duque ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Lymphocyte Proliferation ◽  
Ige Receptors ◽  
B7 Molecules ◽  
Soluble Fusion Protein

Aggregation kinetics in the presence of brain lipids of Aβ(1–40) cleaved from a soluble fusion protein

2018 ◽  
Vol 1860 (9) ◽  
pp. 1681-1686 ◽  
Author(s):  
Miriam A. Kael ◽  
Daniel K. Weber ◽  
Frances Separovic ◽  
Marc-Antoine Sani
Keyword(s):  
Fusion Protein ◽  
Aggregation Kinetics ◽  
Brain Lipids ◽  
Soluble Fusion Protein

scholarly journals Recombinant Adenovirus Expressing a Soluble Fusion Protein PD-1/CD137L Subverts the Suppression of CD8+ T Cells in HCC

2019 ◽  
Vol 27 (11) ◽  
pp. 1906-1918 ◽  
Author(s):  
Yonghui Zhang ◽  
Hailin Zhang ◽  
Mei Wei ◽  
Tao Mou ◽  
Tao Shi ◽  
...  
Keyword(s):  
T Cells ◽  
Fusion Protein ◽  
Cd8 T Cells ◽  
Recombinant Adenovirus ◽  
Soluble Fusion Protein

Enhanced antitumor immunity by fusion of CTLA-4 to a self tumor antigen

Blood ◽  
2000 ◽  
Vol 96 (12) ◽  
pp. 3663-3670 ◽  
Author(s):  
Tzu-Hsuan Huang ◽  
Pin-Yi Wu ◽  
Chin-Nien Lee ◽  
Hsing-I Huang ◽  
Shie-Liang Hsieh ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Tumor Antigen ◽  
Cytotoxic T Lymphocyte ◽  
Specific Antigen ◽  
Activated T Cells ◽  
B Cell Malignancy ◽  
B7 Molecules ◽  
Antigen Presenting ◽  
Id Protein

Abstract The idiotypic determinant (Id) of the immunoglobulin expressed by a B-cell malignancy can serve as an effective tumor-specific antigen but is only weakly immunogenic. This study demonstrates that the immunogenicity of the tumor Id protein can be dramatically increased by directing it to antigen-presenting cells (APCs). Cytotoxic T-lymphocyte antigen 4 (CTLA-4) present on activated T cells has a strong binding affinity to both B7-1 and B7-2 molecules, which are primarily expressed on APCs. After construction of a fusion protein consisting of Id and CTLA-4 (Id-CTLA4), mice immunized with the fusion protein induced high titers of Id-specific antibody and T-cell proliferative responses without adjuvants and were protected from lethal tumor challenge. The Id-CTLA4 fusion protein was so potent that even low doses (down to 0.1 μg) of the immunogen were able to elicit strong antibody responses. By using an Id-CTLA4 mutant protein, the ability to bind B7 molecules on APCs was shown to be required for the enhanced immunogenicity of Id-CTLA4. These findings demonstrate that fusing CTLA-4 to a potential tumor antigen represents an effective approach to prime antitumor immunities in vivo and may be applicable to the design of vaccines for a variety of other diseases.

scholarly journals Human Metapneumovirus Reinfection among Children in Thailand Determined by ELISA Using Purified Soluble Fusion Protein

2008 ◽  
Vol 198 (6) ◽  
pp. 836-842 ◽  
Author(s):  
Julie A. Pavlin ◽  
Andrew C. Hickey ◽  
Nancy Ulbrandt ◽  
Yee‐Peng Chan ◽  
Timothy P. Endy ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Human Metapneumovirus ◽  
Soluble Fusion Protein

cDNA cloning and prokaryotic expression of β-glucosidase in tea plant [Camellia sinensis (L.) O. Kutze]

2005 ◽  
Vol 2 (2) ◽  
pp. 107-111 ◽  
Author(s):  
Jiang Chang-Jun ◽  
Li Yuan-Hua ◽  
Fang Wan-Ping
Keyword(s):  
Fusion Protein ◽  
Camellia Sinensis ◽  
Prokaryotic Expression ◽  
Cdna Sequence ◽  
Expression System ◽  
Tea Plant ◽  
Aroma Precursors ◽  
Soluble Fusion Protein ◽  
Α Helix ◽  
Pleated Sheet

AbstractThe β-glucosidase gene has important effects on alcoholic aroma precursors and insect resistance of the tea plant [Camellia sinensis (L.) O. Kutze]. The complete cDNA sequence of β-glucosidase of the tea plant was cloned; its full length was 1475 bp, and shared 40–60% similarity with corresponding parts of the nucleotide sequence of β-glucosidase gene from other plants. Its secondary structure contains 14.33% α-helix, 25.43% β-pleated sheet and many functional amino acid domains. The β-glucosidase gene was cloned into the pET-32a expression system and expressed at high-efficiently in Escherichia coli BL21 (DE3); the molecular weight of expressed fusion protein was 63 kDa. The results of enzymic reaction showed that the fusion protein possessed normal bioactivity, and it could catalyse the dehydration of the glycosidic bond. The soluble fusion protein was expressed mainly in the cytoplasm.

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