Generation and characterization of a recombinant antibody fragment that binds to the coat protein of grapevine leafroll-associated virus 3

2008 ◽  
Vol 153 (6) ◽  
pp. 1075-1084 ◽  
Author(s):  
Martin Orecchia ◽  
Greta Nölke ◽  
Pasquale Saldarelli ◽  
Mariangela Dell’Orco ◽  
Kerstin Uhde-Holzem ◽  
...  
Keyword(s):  
Coat Protein ◽  
Recombinant Antibody ◽  
Antibody Fragment ◽  
Recombinant Antibody Fragment

Conjugation of an antibody Fv fragment to a virus coat protein: cell-specific targeting of recombinant polyoma-virus-like particles

2001 ◽  
Vol 356 (3) ◽  
pp. 867-873 ◽  
Author(s):  
Kay STUBENRAUCH ◽  
Stefan GLEITER ◽  
Ulrich BRINKMANN ◽  
Rainer RUDOLPH ◽  
Hauke LILIE
Keyword(s):  
Coat Protein ◽  
Mammalian Cells ◽  
Recombinant Antibody ◽  
Specific Antigen ◽  
Antibody Fragment ◽  
Fusion Peptides ◽  
Virus Like Particles ◽  
Vector Systems ◽  
Virus Coat

The development of cell-type-specific delivery systems is highly desirable for gene-therapeutic applications. Current virus-based vector systems show broad cell specificity, which results in the need to restrict the natural tropism of these viral systems. Here we demonstrate that tumour-cell-specific virus-like particles can be functionally assembled in vitro from recombinant viral coat protein expressed in Escherichia coli. The insertion of a negatively charged peptide in the HI loop of polyoma VP1 interferes with the binding of VP1 to the natural recognition site on mammalian cells and also serves as an adapter for the coupling of antibody fragments that contain complementary charged fusion peptides. A recombinant antibody fragment of the tumour-specific anti-(Lewis Y) antibody B3 could be coupled to the mutant VP1 by engineered polyionic peptides and an additional disulphide bond. With this system an entirely recombinant cell-specific delivery system assembled in vitro could be generated that transfers genes preferentially to cells presenting the tumour-specific antigen on the cell surface.

High-level accumulation of a recombinant antibody fragment in the periplasm ofEscherichia coli requires a triple-mutant (degP prc spr) host strain

2004 ◽  
Vol 85 (5) ◽  
pp. 463-474 ◽  
Author(s):  
Christina Chen ◽  
Brad Snedecor ◽  
Julie C. Nishihara ◽  
John C. Joly ◽  
Nancy McFarland ◽  
...  
Keyword(s):  
Recombinant Antibody ◽  
Antibody Fragment ◽  
Ofescherichia Coli ◽  
Host Strain ◽  
Triple Mutant ◽  
Recombinant Antibody Fragment ◽  
High Level

scholarly journals Isolation and Characterisation of a Recombinant Antibody Fragment That Binds NCAM1-Expressing Intervertebral Disc Cells

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e83678 ◽  
Author(s):  
Claire Cunningham ◽  
Akshay Srivastava ◽  
Estelle Collin ◽  
Sibylle Grad ◽  
Mauro Alini ◽  
...  
Keyword(s):  
Intervertebral Disc ◽  
Recombinant Antibody ◽  
Antibody Fragment ◽  
Recombinant Antibody Fragment ◽  
Disc Cells

scholarly journals Production of a Soluble Recombinant Antibody Fragment against MMP9 Using Escherichia coli

Medicina ◽  
2021 ◽  
Vol 57 (9) ◽  
pp. 981
Author(s):  
Chang-Hun Yeom ◽  
Hee-Jin Jeong
Keyword(s):  
Escherichia Coli ◽  
Recombinant Antibody ◽  
Antibody Fragment ◽  
Soluble Form ◽  
Efficient Production ◽  
Binding Ability ◽  
Recombinant Scfv ◽  
Recombinant Antibody Fragment ◽  
Recombinant Antibody Fragments ◽  
Metalloproteinase 9

Matrix metalloproteinase 9 (MMP9) is involved in several aspects of the pathology of cancer, including invasion, metastasis, and angiogenesis. In this study, we expressed a recombinant scFv-type anti-MMP9 antibody in soluble form using Escherichia coli, purified it, and confirmed its antigen-binding ability. The convenient, rapid, inexpressive system used in this study for producing recombinant antibody fragments needs only five days, and thus can be used for the efficient production of scFv against MMP9, which can be used in a range of applications and industrial fields, including diagnosis and treatment of inflammatory and cancer-related diseases.

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