scholarly journals Production, purification, and characterization of a fusion protein of carbonic anhydrase fromNeisseria gonorrhoeaeand cellulose binding domain fromClostridium thermocellum

2009 ◽  
Vol 25 (1) ◽  
pp. 68-74 ◽  
Author(s):  
Zhu Liu ◽  
Patrick Bartlow ◽  
Robert M. Dilmore ◽  
Yee Soong ◽  
Zhiwei Pan ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Fusion Protein ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Purification And Characterization ◽  
Cellulose Binding

scholarly journals Cellulose as an inert matrix for presenting cytokines to target cells: production and properties of a stem cell factor–cellulose-binding domain fusion protein

1999 ◽  
Vol 339 (2) ◽  
pp. 429-434
Author(s):  
J. Greg DOHENY ◽  
Eric J. JERVIS ◽  
M. Marta GUARNA ◽  
R. Keith HUMPHRIES ◽  
R. Antony J. WARREN ◽  
...  
Keyword(s):  
Stem Cell ◽  
Fusion Protein ◽  
Stem Cell Factor ◽  
Direct Analysis ◽  
Binding Domain ◽  
Target Cells ◽  
Cellulose Binding Domain ◽  
Binding Characteristics ◽  
Cellulose Binding ◽  
Cellulose Surface

A chimaera of stem cell factor (SCF) and a cellulose-binding domain from the xylanase Cex (CBDCex) effectively immobilizes SCF on a cellulose surface. The fusion protein retains both the cytokine properties of SCF and the cellulose-binding characteristics of CBDCex. When adsorbed on cellulose, SCF–CBDCex is up to 7-fold more potent than soluble SCF–CBDCex and than native SCF at stimulating the proliferation of factor-dependent cell lines. When cells are incubated with cellulose-bound SCF–CBDCex, activated receptors and SCF–CBDCex co-localize on the cellulose matrix. The strong binding of SCF–CBDCex to the cellulose surface permits the effective and localized stimulation of target cells; this is potentially significant for long-term perfusion culturing of factor-dependent cells. It also permits the direct analysis of the effects of surface-bound cytokines on target cells.

scholarly journals Cellulose as an inert matrix for presenting cytokines to target cells: production and properties of a stem cell factor‒cellulose-binding domain fusion protein

1999 ◽  
Vol 339 (2) ◽  
pp. 429 ◽  
Author(s):  
J. Greg DOHENY ◽  
Eric J. JERVIS ◽  
M. Marta GUARNA ◽  
R. Keith HUMPHRIES ◽  
R. Antony J. WARREN ◽  
...  
Keyword(s):  
Stem Cell ◽  
Fusion Protein ◽  
Stem Cell Factor ◽  
Binding Domain ◽  
Target Cells ◽  
Cellulose Binding Domain ◽  
Inert Matrix ◽  
Domain Fusion ◽  
Cellulose Binding

scholarly journals Stable linker peptides for a cellulose-binding domain–lipase fusion protein expressed in Pichia pastoris

2001 ◽  
Vol 14 (9) ◽  
pp. 711-715 ◽  
Author(s):  
Malin Gustavsson ◽  
Janne Lehtiö ◽  
Stuart Denman ◽  
Tuula T. Teeri ◽  
Karl Hult ◽  
...  
Keyword(s):  
Pichia Pastoris ◽  
Fusion Protein ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Linker Peptides ◽  
Cellulose Binding

Nanobody-Functionalized Cellulose for Capturing SARS-CoV-2

2022 ◽  
Author(s):  
Xin Sun ◽  
Shaobo Yang ◽  
Amal A. Al-Dossary ◽  
Shana Broitman ◽  
Yun Ni ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Cost Effective ◽  
Binding Domain ◽  
Receptor Binding Domain ◽  
Cellulose Binding Domain ◽  
Viral Spread ◽  
Cellulose Substrates ◽  
Bifunctional Fusion Protein ◽  
Cellulose Binding ◽  
Cellulose Materials

The highly transmissible severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has infected more than 253 million people, claiming ∼ 5.1 million lives to date. Although mandatory quarantines, lockdowns, and vaccinations help curb viral transmission, there is a pressing need for cost-effective systems to mitigate the viral spread. Here, we present a generic strategy for capturing SARS-CoV-2 through functionalized cellulose materials. Specifically, we developed a bifunctional fusion protein consisting of a cellulose-binding domain and a nanobody (Nb) targeting the receptor-binding domain of SARS-CoV-2. The immobilization of the fusion proteins on cellulose substrates enhanced the capture efficiency of Nbs against SARS-CoV-2 pseudoviruses of the wildtype and the D614G variant, the latter of which has been shown to confer higher infectivity. Furthermore, the fusion protein was integrated into a customizable chromatography with highly porous cellulose to capture viruses from complex fluids in a continuous fashion. By capturing and containing viruses through the Nb-functionalized cellulose, our work may find utilities in virus sampling and filtration towards paper-based diagnostics, environmental tracking of viral spread and reducing viral load from infected individuals. IMPORTANCE The ongoing efforts to address the COVID-19 pandemic center around the development of diagnostics, preventative measures, and therapeutic strategies. In comparison to existing work, we have provided a complementary strategy to capture SARS-CoV-2 by functionalized cellulose materials towards paper-based diagnostics as well as virus filtration in perishable samples. Specifically, we developed a bifunctional fusion protein consisting of both a cellulose-binding domain and a nanobody specific for the receptor-binding domain of SARS-CoV-2. As a proof-of-concept, the fusion protein-coated cellulose substrates exhibited enhanced capture efficiency against SARS-CoV-2 pseudovirus of both wildtype and the D614G mutant variants, the latter of which has been shown to confer higher infectivity. Furthermore, the fusion protein was integrated into a customizable chromatography for binding viruses from complex biological fluids in a highly continuous and cost-effective manner. Such antigen-specific capture can potentially immobilize viruses of interest for viral detection and removal, which contrasts with the common size- or affinity-based filtration devices that bind a broad range of bacteria, viruses, fungi, and cytokines present in blood ( https://clinicaltrials.gov/ct2/show/NCT04413955 ). Additionally, since our work focuses on capturing and concentrating viruses from surfaces and fluids as a means to improve detection, it can serve as an “add-on” technology to complement existing viral detection methods, many of which have been largely focusing on improving the intrinsic sensitivities.

The cellulose-binding domain (CBDCex) of an exoglucanase fromCellulomonas fimi: Production inEscherichia coli and characterization of the polypeptide

1993 ◽  
Vol 42 (4) ◽  
pp. 401-409 ◽  
Author(s):  
Edgar Ong ◽  
Neil R. Gilkes ◽  
Robert C. Miller ◽  
R. Antony J. Warren ◽  
Douglas G. Kilburn
Keyword(s):  
Binding Domain ◽  
Inescherichia Coli ◽  
Cellulose Binding Domain ◽  
Cellulose Binding

scholarly journals Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A.

1993 ◽  
Vol 175 (18) ◽  
pp. 5762-5768 ◽  
Author(s):  
M A Goldstein ◽  
M Takagi ◽  
S Hashida ◽  
O Shoseyov ◽  
R H Doi ◽  
...  
Keyword(s):  
Binding Protein ◽  
Protein A ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Clostridium Cellulovorans ◽  
Cellulose Binding

A streptavidin-cellulose-binding domain fusion protein that binds biotinylated proteins to cellulose

1994 ◽  
Vol 16 (6) ◽  
pp. 496-500 ◽  
Author(s):  
Khai D. Le ◽  
Neil R. Gilkes ◽  
Douglas G. Kilburn ◽  
Robert C. Miller ◽  
John N. Saddler ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Binding Domain ◽  
Cellulose Binding Domain ◽  
Domain Fusion ◽  
Cellulose Binding
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