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Carbohydrate binding module-fused antibodies improve the performance of cellulose-based lateral flow immunoassays.
- Source :
-
Scientific reports [Sci Rep] 2021 Apr 12; Vol. 11 (1), pp. 7880. Date of Electronic Publication: 2021 Apr 12. - Publication Year :
- 2021
-
Abstract
- Since the pandemic outbreak of Covid-19 in December 2019, several lateral flow assay (LFA) devices were developed to enable the constant monitoring of regional and global infection processes. Additionally, innumerable lateral flow test devices are frequently used for determination of different clinical parameters, food safety, and environmental factors. Since common LFAs rely on non-biodegradable nitrocellulose membranes, we focused on their replacement by cellulose-composed, biodegradable papers. We report the development of cellulose paper-based lateral flow immunoassays using a carbohydrate-binding module-fused to detection antibodies. Studies regarding the protein binding capacity and potential protein wash-off effects on cellulose paper demonstrated a 2.7-fold protein binding capacity of CBM-fused antibody fragments compared to the sole antibody fragment. Furthermore, this strategy improved the spatial retention of CBM-fused detection antibodies to the test area, which resulted in an enhanced sensitivity and improved overall LFA-performance compared to the naked detection antibody. CBM-assisted antibodies were validated by implementation into two model lateral flow test devices (pregnancy detection and the detection of SARS-CoV-2 specific antibodies). The CBM-assisted pregnancy LFA demonstrated sensitive detection of human gonadotropin (hCG) in synthetic urine and the CBM-assisted Covid-19 antibody LFA was able to detect SARS-CoV-2 specific antibodies present in serum. Our findings pave the way to the more frequent use of cellulose-based papers instead of nitrocellulose in LFA devices and thus potentially improve the sustainability in the field of POC diagnostics.
- Subjects :
- Biocompatible Materials
Chorionic Gonadotropin chemistry
Clostridium thermocellum immunology
Humans
Immunoglobulin Fragments chemistry
Immunoglobulin G chemistry
Point-of-Care Systems
Protein Binding
SARS-CoV-2 immunology
Urinalysis
Antibodies, Viral analysis
COVID-19 diagnosis
COVID-19 Serological Testing methods
Carbohydrates chemistry
Collodion chemistry
Immunoassay methods
Subjects
Details
- Language :
- English
- ISSN :
- 2045-2322
- Volume :
- 11
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Scientific reports
- Publication Type :
- Academic Journal
- Accession number :
- 33846482
- Full Text :
- https://doi.org/10.1038/s41598-021-87072-7