Lectin-based lateral flow assay: proof-of-concept

• Published in: Analyst (London) Vol. 141; no. 23; pp. 6444 - 6448
• Main Authors: Damborský, Pavel, Koczula, Katarzyna M, Gallotta, Andrea, Katrlík, Jaroslav
• Format: Journal Article
• Language: English
• Published: England 14.11.2016
• Subjects: Antigens; Assaying; Biomarkers; Biomarkers, Tumor - analysis; Glycosylation; Humans; Lectins; Lectins - chemistry; Male; Markers; N-Acetylneuraminic Acid - analysis; Proof of Concept Study; Prostate; Prostate-Specific Antigen - analysis; Prostatic Neoplasms - diagnosis; Sambucus - chemistry; Sampling
• ISSN: 0003-2654; 1364-5528
• DOI: 10.1039/c6an01746k

Lateral flow assays (LFAs) enable the simple and rapid detection and quantification of analytes and is popular for point-of-care (PoC), point-of-use and outdoor testing applications. LFAs typically depend on antibody or nucleic acid based recognition. We present the innovative concept of a LFA using lectins in the role of the biorecognition element. Lectins are a special kind of glycan-binding protein and the lectin-based LFA herein described was developed for the determination of the glycosylation of free prostate specific antigen (PSA). PSA is routinely used as a biomarker of prostate cancer (PCa) and the glycosylation status of PSA is a more specific marker of disease progress than only the PSA level. Using the lectin-based LFA we were able to detect α-2,6 sialic acid present in fPSA using Sambucus nigra (SNA) lectin. As a negative control, we employed Maackia amurensis lectin II (MAA II) which specifically binds α-2,3 sialic acid. The novel approach presented here can be applied to a wide range of biomarkers that have a significant impact on clinical diagnosis and prognosis, providing an alternative to standard lectin-based assays. The assay uses commercial components and is easily performed by applying a sample to the sampling pad on the lectin-based LFA strip, with results obtained within 10 minutes. We present the innovative concept of a LFA using lectins in the role of the biorecognition element for glycoprofiling of biomarkers.