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Biosensors
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Enzyme-linked Immunoassay
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Enzyme-linked Immunoassay

A special issue of Biosensors (ISSN 2079-6374).

Deadline for manuscript submissions: closed (30 April 2019) | Viewed by 11900

Special Issue Editors

Prof. Dr. Claudio Baggiani

E-Mail Website
Guest Editor
Department of Chemistry, University of Turin, 10125 Turin, Italy
Interests: molecular imprinting; ion imprinting; molecular recognition; immunoassay
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Laura Anfossi

E-Mail Website
Guest Editor
Department of Chemistry, Universita degli Studi di Torino, 10124 Torino, Italy
Interests: analytical chemistry; immunochemical assays; food chemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Enzyme-Linked ImmunoSorbent Assays (ELISA) have been in use for decades in the medical area and have become increasingly popular as an efficient analytical method for a number of field of application, thanks to their simplicity, speed, low costs, specificity and sensitivity. Nowadays ELISA are largely applied for pharmaceutical, biological, food, forensic and environmental analysis. ELISA relies on the molecular recognition properties of antibodies and on the signal amplification generated by enzymatic probes that also provide versatile detection, by using chromogenic, fluorescent, and chemiluminescent substrates. Although ELISA principles are very well-known, its expanding application to unexplored fields and the requirement for improved sensitivity, rapidity, reliability, and validity are prompting innovation in the domain. Also, advances on artificial receptors (aptamers, molecular imprinted polymers) and novel probes (DNAzyme, inorganic enzyme mimics) are offering ELISA untried opportunities and challenges to further development. The Special issue will cover advances in hapet design, recognition elements, probes, and assay design with emphasis on strategies for improving sensitivity and for expanding application of ELISA to unusual fields of analysis. The special issue also intends to point out benefits of ELISA for improving access to efficient monitoring and for managing large numbers of analysis in the ‘big data’ era.

Prof. Dr. Claudio Baggiani
Prof. Laura Anfossi
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biosensors is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Enzyme-linked immunoSorbent Assay
  • Immunoassay
  • Nanobody
  • Broad-specific antibodies
  • Artificial antibodies
  • Aptamers
  • Peroxidase mimic
  • DNAzyme
  • Hapten design
  • High-throughput analysis
  • Immuno-PCR

Published Papers (2 papers)

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Research

12 pages, 2354 KiB  
Article
Noncompetitive Chromogenic Lateral-Flow Immunoassay for Simultaneous Detection of Microcystins and Nodularin
by Sultana Akter, Teemu Kustila, Janne Leivo, Gangatharan Muralitharan, Markus Vehniäinen and Urpo Lamminmäki
Biosensors 2019, 9(2), 79; https://0-doi-org.brum.beds.ac.uk/10.3390/bios9020079 - 18 Jun 2019
Cited by 20 | Viewed by 6263
Abstract
Cyanobacterial blooms cause local and global health issues by contaminating surface waters. Microcystins and nodularins are cyclic cyanobacterial peptide toxins comprising numerous natural variants. Most of them are potent hepatotoxins, tumor promoters, and at least microcystin-LR is possibly carcinogenic. In drinking water, the [...] Read more.
Cyanobacterial blooms cause local and global health issues by contaminating surface waters. Microcystins and nodularins are cyclic cyanobacterial peptide toxins comprising numerous natural variants. Most of them are potent hepatotoxins, tumor promoters, and at least microcystin-LR is possibly carcinogenic. In drinking water, the World Health Organization (WHO) recommended the provisional guideline value of 1 µg/L for microcystin-LR. For water used for recreational activity, the guidance values for microcystin concentration varies mostly between 4–25 µg/L in different countries. Current immunoassays or lateral flow strips for microcystin/nodularin are based on indirect competitive method, which are generally more prone to sample interference and sometimes hard to interpret compared to two-site immunoassays. Simple, sensitive, and easy to interpret user-friendly methods for first line screening of microcystin/nodularin near water sources are needed for assessment of water quality and safety. We describe the development of a two-site sandwich format lateral-flow assay for the rapid detection of microcystins and nodularin-R. A unique antibody fragment capable of broadly recognizing immunocomplexes consisting of a capture antibody bound to microcystins/nodularin-R was used to develop the simple lateral flow immunoassay. The assay can visually detect the major hepatotoxins (microcystin-LR, -dmLR, -RR, -dmRR, -YR, -LY, -LF -LW, and nodularin-R) at and below the concentration of 4 µg/L. The signal is directly proportional to the concentration of the respective toxin, and the use of alkaline phosphatase activity offers a cost efficient alternative by eliminating the need of toxin conjugates or other labeling system. The easy to interpret assay has the potential to serve as a microcystins/nodularin screening tool for those involved in water quality monitoring such as municipal authorities, researchers, as well as general public concerned of bathing water quality. Full article
(This article belongs to the Special Issue Enzyme-linked Immunoassay)
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14 pages, 1174 KiB  
Article
Specific and Generic Immunorecognition of Glycopeptide Antibiotics Promoted by Unique and Multiple Orientations of Hapten
by Maksim A. Burkin, Inna A. Galvidis and Sergei A. Eremin
Biosensors 2019, 9(2), 52; https://0-doi-org.brum.beds.ac.uk/10.3390/bios9020052 - 04 Apr 2019
Cited by 7 | Viewed by 5013
Abstract
Conjugation chemistry does not always provide adequate spatial orientation of hapten in immunogens for the best presentation of generic or individual epitopes. In the present study, the influence of unique and multiple orientations of immunizing hapten on the immune response repertoire was compared [...] Read more.
Conjugation chemistry does not always provide adequate spatial orientation of hapten in immunogens for the best presentation of generic or individual epitopes. In the present study, the influence of unique and multiple orientations of immunizing hapten on the immune response repertoire was compared to select generic recognition system. The glycopeptides, teicoplanin (TPL) and ristomycin (RSM), were conjugated to BSA to produce immunogens with unique and multiple orientations of haptens. Polyclonal antibodies generated against TPL conjugated through a single site were of uniform specificity and demonstrated selective TPL recognition, regardless of the coating conjugates design. The sensitivity (IC50) of 4 enzyme-linked immunosorbent assays (ELISAs) for TPL varied little within the 3.5–7.4 ng/mL, with a dynamic range of 0.2–100 ng/mL. RSM was coupled to BSA through several glycoside sites that evoked a wider repertoire of response. This first described anti-RSM antibody was selective for RSM in homologous hapten-coated ELISAs with IC50 values in the range 4.2–35 ng/mL. Among the heterologous antigens, periodate-oxidized TPL conjugated to gelatine was selected as the best binder of generic anti-RSM fraction. The developed ELISA showed group recognition of glycopeptides RSM, TPL, eremomycin, and vancomycin with cross-reactivity of 37–100% and a 10–10,000 ng/mL dynamic range. Thus, multiple presentations of immunizing hapten help expand the repertoire of immune responses and opportunities for the selection of the required fine-specificity agent. Full article
(This article belongs to the Special Issue Enzyme-linked Immunoassay)
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