2021
DOI: 10.1016/j.snb.2020.129099
|View full text |Cite
|
Sign up to set email alerts
|

A sensitive paper-based lateral flow immunoassay platform using engineered cellulose-binding protein linker fused with antibody-binding domains

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

2
12
0

Year Published

2021
2021
2024
2024

Publication Types

Select...
7
1

Relationship

1
7

Authors

Journals

citations
Cited by 22 publications
(17 citation statements)
references
References 36 publications
2
12
0
Order By: Relevance
“…Furthermore, we found comparable sensitivities, regarding hCG detection using NC-based LFAs (functionalized by anti-hCG scFv) or cellulose-based LFAs (functionalized by CBM-anti-hCG scFv) (Figure S7 ). This indicates that cellulose-based LFAs could reach similar sensitivities compared to common nitrocellulose-based LFAs, when using CBM-fused detection reagents, which is in accordance with recently published data 24 . Furthermore, we observed a dramatic loss of sensitivity of the solitary detection antibodies and antibody fragments on cellulose-based LFAs, compared to the CBM-fused counterparts (Fig.…”
Section: Discussionsupporting
confidence: 92%
See 1 more Smart Citation
“…Furthermore, we found comparable sensitivities, regarding hCG detection using NC-based LFAs (functionalized by anti-hCG scFv) or cellulose-based LFAs (functionalized by CBM-anti-hCG scFv) (Figure S7 ). This indicates that cellulose-based LFAs could reach similar sensitivities compared to common nitrocellulose-based LFAs, when using CBM-fused detection reagents, which is in accordance with recently published data 24 . Furthermore, we observed a dramatic loss of sensitivity of the solitary detection antibodies and antibody fragments on cellulose-based LFAs, compared to the CBM-fused counterparts (Fig.…”
Section: Discussionsupporting
confidence: 92%
“…Recently, a study addressing the applicability of a CBM-fused ZZ-domain for the colorimetric detection of DNA strands on cellulose particles was published by Rosa et al 23 . Additionally, a recently published study addressed the applicability of protein A-derived domains fused to different CBM domains, resulting in improved binding onto cellulose-paper used for lateral flow immuno assays 24 . However, this newly developed platform displayed several limitations including unwanted cross-reactivity to (detection-) antibodies from different species.…”
Section: Introductionmentioning
confidence: 99%
“…The use of biodegradable components could also be desirable, even if most of the LFIAs for professional use (in the clinical field) must be incinerated due to possible biohazard. Notwithstanding the exceptional properties of the nitrocellulose as solid support for the LFIA platform, researchers [ 291 , 292 , 293 ] are trying to replace its use with the cellulose that, in addition to further reducing costs, would have a reduced impact on the environment because its production process requires less chemicals in comparison to the nitrocellulose production. Most recently, promising results have been obtained by Adrian Elter et al that developed cellulose-based LFIAs [ 294 ].…”
Section: Future Perspectivesmentioning
confidence: 99%
“…The recombinant CBP31-BC protein was produced in Escherichia coli as previously described. [26] Recombinant E. coli BL21 (DE3) containing pET-CBP31-BC was grown in 400 mL of LB medium (0.5 % yeast extract, 1 % tryptophan, and 1 % NaCl) with 50 μg/mL ampicillin at 37 °C. When the culture reached an optical density of ∼0.8–0.9 at 600 nm (OD 600 ), 1 mM IPTG was added to induce the expression of CBP31-BC protein.…”
Section: Methodsmentioning
confidence: 99%
“…The protein adsorption capacity of the nitrocellulose membrane makes it difficult to control the orientation of immobilized antibodies [25] . In a previous study, we developed a cellulose membrane-based sensitive lateral flow immunoassay (LFIA) using a bifunctional fusion linker, CBP31-BC, composed of cellulose-binding domains (CBDs) and antibody-binding domains [26] . Due to oriented antibody immobilization on cellulose by CBP31-BC linker, the cellulose membrane-based LFIA showed a ∼10-fold higher sensitivity to prostate-specific antigens than nitrocellulose membrane-based conventional LFIAs.…”
Section: Introductionmentioning
confidence: 99%