Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2024 Jul 25:12:25151355241264520.
doi: 10.1177/25151355241264520. eCollection 2024.

Monoclonal IgY antibodies: advancements and limitations for immunodiagnosis and immunotherapy applications

Ashraf A Tabll  1   2 , Yasser E Shahein  3 , Mohamed M Omran  4 , Nahla A Hussein  3 , Asmaa El-Shershaby  3 , Ana Petrovic  5 , Marija Glasnovic  5 , Robert Smolic  5 , Martina Smolic  6
Affiliations
Review

Monoclonal IgY antibodies: advancements and limitations for immunodiagnosis and immunotherapy applications

Ashraf A Tabll et al. Ther Adv Vaccines Immunother. .

Abstract

Due to their high specificity and scalability, Monoclonal IgY antibodies have emerged as a valuable alternative to traditional polyclonal IgY antibodies. This abstract provides an overview of the production and purification methods of monoclonal IgY antibodies, highlights their advantages over polyclonal IgY antibodies, and discusses their recent applications. Monoclonal recombinant IgY antibodies, in contrast to polyclonal IgY antibodies, offer several benefits. such as derived from a single B-cell clone, monoclonal antibodies exhibit superior specificity, ensuring consistent and reliable results. Furthermore, it explores the suitability of monoclonal IgY antibodies for low- and middle-income countries, considering their cost-effectiveness and accessibility. We also discussed future directions and challenges in using polyclonal IgY and monoclonal IgY antibodies. In conclusion, monoclonal IgY antibodies offer substantial advantages over polyclonal IgY antibodies regarding specificity, scalability, and consistent performance. Their recent applications in diagnostics, therapeutics, and research highlight their versatility.

Keywords: IgY antibodies; chicken egg yolk antibodies; hybridoma technology; immunodiagnosis; immunotherapy; monoclonal antibodies; pandemics.

Plain language summary

Chicken egg yolk antibodies (IgY) and monoclonal antibodies: advancements and limitations for immunodiagnosis and immunotherapy applications Chicken egg yolk antibodies (IgY antibodies) and monoclonal antibodies (mAbs) are two types of antibodies used in medical applications. IgY antibodies are cost-effective, stable, and specific, with the advantage of not triggering harmful immune responses. However, they may have limitations in identifying certain target areas and availability. On the other hand, mAbs are highly specific and can detect multiple target areas on antigens, but their production is expensive and may cause immune responses. Despite these drawbacks, both IgY antibodies and mAbs show promise in various applications such as infectious disease diagnosis, cancer treatment, and autoimmune disorders. Ongoing developments in antibody technology are likely to expand their applications in immunology. This review provides an overview of the strengths and limitations of IgY antibodies and mAbs in immunodiagnosis and immunotherapy, as well as their role in pandemic control.

PubMed Disclaimer

Figures

Figure 1.
Figure 1.
Comparison between mammalian IgG and Avian IgY different biochemical structures and properties. IgY contains two glycosylation sites at the Cυ2 and Cυ3 while the IgG contains only one at the Cγ2. Source. The antibodies diagrams were created using BioRender.com.
Figure 2.
Figure 2.
Diagrammatic procedures for the production of chicken egg polyclonal IgY. Source. The figure is created using BioRender.com.
Figure 3.
Figure 3.
Protein and lipid content of egg yolk and main steps of IgY purification.
Figure 4.
Figure 4.
The most common approaches to generate monoclonal IgY (mIgY). Source. The figure is created using BioRender.com.
Figure 5.
Figure 5.
ADLib principle using DT0 cells. Source. The figure is created using BioRender.com.
Figure 6.
Figure 6.
Saccharomyces cerevisiae surface display approach of scFv. Source. The figure is created using BioRender.com.
Figure 7.
Figure 7.
Potential applications of IgY technology.
Figure 8.
Figure 8.
Different epitopes were identified on the S protein of SARS-CoV-2 and have significant binding to IgY. Source. Figure is created using BioRender.com. FP, fusion protein; HR1 and HR2, heptad repeat 1 and 2; I.T, the intracellular tail; NTD, the N-terminal domain; RBD, receptor binding domain; T.A: transmembrane anchor.
Figure 9.
Figure 9.
IgY-targeted veterinary diseases.
See this image and copyright information in PMC

References

    1. Suresh LG, Indhuprakash ST, Gandhi S, et al. Amalgamation of nanotechnology with chicken IgY to enrich therapeutic and diagnostic applications: a systematic review. Immunotherapy 2023; 15: 867–884. - PubMed
    1. Ren H, Yang W, Thirumalai D, et al. A comparative evaluation of six principal IgY antibody extraction methods. Altern Lab Anim 2016; 44: 11–20. - PubMed
    1. Karachaliou CE, Vassilakopoulou V, Livaniou E. IgY technology: methods for developing and evaluating avian immunoglobulins for the in vitro detection of biomolecules. World J Methodol 2021; 11: 243–262. - PMC - PubMed
    1. León-Núñez D, Vizcaíno-López MF, Escorcia M, et al. IgY antibodies as biotherapeutics in biomedicine. Antibodies (Basel) 2022; 11: 62. - PMC - PubMed
    1. Chiu ML, Goulet DR, Teplyakov A, et al. Antibody structure and function: the basis for engineering therapeutics. Antibodies (Basel) 2019; 8: 55. - PMC - PubMed

LinkOut - more resources