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IgY technology refers to the strategic production process involved in generating avian immunoglobulin (IgY) against target antigens in a much more cost-effective manner with broad applications in the fields of diagnostics, prophylaxis, and therapeutics for both human and veterinary medicine. Over the past decade, promising progress in this research area has been evident from the steep increase in the number of registered manufacturing companies involved in the production of IgY products, the number of patents, and the notable number of clinical trials underway. Hence, it is crucial to conduct a prospective analysis of the commercialization and marketing potential of IgY-based commercial products for large-scale applications. This review revealed that the number of IgY patent applications increased steeply after 2010, with the highest of 77 patents filed in 2021. In addition, 73 industries are reportedly involved in marketing IgY products, out of which 27 were promoting biotherapeutics for human and veterinary medicine and 46 were in the diagnostic field. IgY antibodies are being used as primary and secondary antibodies, with approximately 3729 and 846 products, respectively. Biotherapeutic product consumption has notably increased as a food supplement and as a topical application in human and veterinary medicine, which are under different clinical phases of development to reach the market with around 80 and 56 products, respectively. In contrast, the number of IgY products as parenteral administrations and licensed drugs is not well developed given the lack of technical standards established for IgY registration and industrialization, as well as the restriction of the nature of polyclonal antibodies. However, recent ongoing research on functional IgY fragments indicates a promising area for IgY applications in the near future. Therefore, retrospective analysis with speculations is mandatory for IgY technology maturation toward industrialization and commercialization.

As severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to spread globally, a series of vaccines, antibodies and drugs have been developed to combat coronavirus disease 2019 (COVID-19). High specific antibodies are powerful tool for the development of immunoassay and providing passive immunotherapy against SARS-CoV-2 and expected with large scale production. SARS-CoV-2 S1 protein was expressed in E. coli BL21 and purified by immobilized metal affinity chromatography, as antigen used to immunize hens, the specific IgY antibodies were extracted form egg yolk by PEG-6000 precipitation, and the titer of anti-S1 IgY antibody reached 1:10,000. IgY single chain variable fragment antibody (IgY-scFv) was generated by using phage display technology and the IgY-scFv showed high binding sensitivity and capacity to S1 protein of SARS-CoV-2, and the minimum detectable antigen S1 protein concentration was 6 ng/µL. The docking study showed that the multiple epitopes on the IgY-scFv interacted with multiple residues on SARS-CoV-2 S1 RBD to form hydrogen bonds. This preliminary study suggests that IgY and IgY-scFv are suitable candidates for the development of immunoassay and passive immunotherapy for COVID-19 to humans and animals.

An approach toward novel neutralizing IgY polyclonal antibodies (N-IgY-pAb) against SARS-CoV-2 S-ECD was developed. The novel N-IgY-pAb and its intranasal spray response against the wild type (\"'WH-Human 1\") SARS-CoV-2 virus, variants of Delta or Omicron were up to 98%. Unique virus peptides binding to N-IgY-pAb were screened by a SARS-CoV-2 proteome microarray. Seventeen mutation-free peptides with a Z-score > 3.0 were identified as potent targets from a total of 966 peptides. The new findings show that one is in the RBM domain ( LKPFERDISTEIYQA ), two are in the NTD domain ( RTQLPPAYTNSFTRG , CALDPLSETKCTLKS ) four are in the C1/2-terminal ( PFQQFGRDIADTTDA , DTTDAVRDPQTLEIL , TLEILDITPCSFGGV , ECDIPIGAGICASYQ ), three are in the S1/S2 border ( YICGDSTECSNLLLQ , KPSKRSFIEDLLFNK , LLFNKVTLADAGFIK ) one target is in HR2 ( SPDVDLGDISGINAS ) and one is in HR2-TM ( QELGKYEQYIKWPWY ). Moreover, five potential peptides were in the NSP domain: nsp3-55 ( SNEKQEILGTVSWNL ), nsp14-50 ( HHANEYRLYLDAYNM , ORF10-3 ( MNSRNYIAQVDVVNFNLT , ORF7a-1( MKIILFLALITLATC ) and ORF7a-12 ( TLCFTLKRKTE ). We concluded that the N-IgY-pAb could effectively neutralize the SARS-CoV-2. The new findings of seventeen potent conserved peptides are extremely important for developing new vaccines and \"cocktails\" of neutralizing Abs for efficient treatments for patients infected with SARS-CoV-2.

Antibody mimetics may be used for various biomedical applications, especially those for which conventional antibodies are ineffective. In this study, we developed a smaller molecular chicken IgY mimetic peptide (IgY-peptide) based on the complementarity-determining regions (CDRs) of the anti-canine parvovirus (CPV) IgY-scFv prepared previously. The mimetic peptide showed no cross-reactivity with canine distemper virus (CDV) and canine coronavirus (CCV) and showed excellent protective properties for Crandell-Rees Feline Kidney (CRFK) cells against CPV. This study is the first attempt to develop a mimetic IgY-peptide and demonstrates the ease and feasibility in generating such a novel antibody-like functional molecule for biomedical purposes.

There has been an increasing interest in using Immunoglobulin Y (IgY) antibodies as an alternative to “classical” antimicrobials. Unlike traditional antibiotics, they can be utilized on a continual basis without leading to the development of resistance. The veterinary IgY antibody market is growing because of the demand for minimal antibiotic use in animal production. IgY antibodies are not as strong as antibiotics for treating infections, but they work well as preventative agents and are natural, nontoxic, and easy to produce. They can be administered orally and are well tolerated, even by young animals. Unlike antibiotics, oral IgY supplements support the microbiome that plays a vital role in maintaining overall health, including immune system function. IgY formulations can be delivered as egg yolk powder and do not require extensive purification. Lipids in IgY supplements improve antibody stability in the digestive tract. Given this, using IgY antibodies as an alternative to antimicrobials has garnered interest. In this review, we will examine their antibacterial potential.

Antiviral, antibacterial, and antiparasitic drugs and vaccines are essential to maintaining the health of humans and animals. Yet, their production can be slow and expensive, and efficacy lost once pathogens mount resistance. Chicken immunoglobulin Y (IgY) is a highly conserved homolog of human immunoglobulin G (IgG) that has shown benefits and a favorable safety profile, primarily in animal models of human infectious diseases. IgY is fast-acting, easy to produce, and low cost. IgY antibodies can readily be generated in large quantities with minimal environmental harm or infrastructure investment by using egg-laying hens. We summarize a variety of IgY uses, focusing on their potential for the detection, prevention, and treatment of human and animal infections.

Introduction: The coronavirus disease 2019 (COVID-19) pandemic has significantly accelerated the development of diagnostic techniques. Real‑time quantitative polymerase chain reaction (RT‑qPCR) was the method of choice for diagnosis and was considered as the gold standard. However, limited specificity of RT-PCR was noticed during the pandemic. This research aimed to develop a combined highly specific immune-based and highly sensitive molecular-based diagnostic technique. Methodology: Groups of chicken were immunized with commercial severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) N, S, and E antigens. The IgY antibodies were purified from eggs using a High-Trap IgY affinity column. Three unique DNA barcodes were designed, synthesized, and amplified using 5′-amine–labeled forward primers. DNA barcodes purified form PCR products were coupled to IgY antibodies using the (1-ethyl-3-(3-dimethylaminopropyl)carbodiimide) - N-hydroxysuccinimide (EDC-NHS) coupling chemistry. ELISA; SDS-PAGEs; immunoblot (IB); and uniplex-, duplex- and multiplex immuno-PCR (IPCR) were used to confirm system validity. Results: Amplification of single barcodes using RT-PCR showed a Ct value of 15, with no significant variation when amplified in duplex or multiplex formats. Chicken IgY–DNA barcode conjugation and reactivity were verified using IB and ELISA. IPCR resulted in efficient amplification of all three DNA barcodes in uniplex, duplex, and multiplex formats after binding to commercial N, S, and E antigens. Conclusions: The successful combination of the specific antibody-based techniques, low-cost chicken IgY antibodies, and RT-PCR sensitivity achieved in this study present a promising approach to meet the demand for sensitive and accurate diagnostics. This generic platform can be adopted in any analyte detection system.

Antibiotic resistant bacteria are a growing threat to global health security. Whilst the emergence of antimicrobial resistance (AMR) is a natural phenomenon, it is also driven by antibiotic exposure in health care, agriculture, and the environment. Antibiotic pressure and inappropriate use of antibiotics are important factors which drive resistance. Apart from their use to treat bacterial infections in humans, antibiotics also play an important role in animal husbandry. With limited antibiotic options, alternate strategies are required to overcome AMR. Passive immunization through oral, nasal and topical administration of egg yolk-derived IgY antibodies from immunized chickens were recently shown to be effective for treating bacterial infections in animals and humans. Immunization of chickens with specific antigens offers the possibility of creating specific antibodies targeting a wide range of antibiotic-resistant bacteria. In this review, we describe the growing global problem of antimicrobial resistance and highlight the promising potential of the use of egg yolk IgY antibodies for the treatment of bacterial infections, particularly those listed in the World Health Organization priority list.

The emergence of SARS-CoV-2 in late 2019 initiated a global pandemic, which led to a need for effective therapeutics and diagnostic tools, including virus-specific antibodies. Here, we investigate different antigen preparations to produce SARS-CoV-2-specific and virus-neutralizing antibodies in chickens (n = 3/antigen) and rabbits (n = 2/antigen), exploring, in particular, egg yolk for large-scale production of immunoglobulin Y (IgY). Reactivity profiles of IgY preparations from chicken sera and yolk and rabbit sera were tested in parallel. We compared three types of antigens based on ancestral SARS-CoV-2: an inactivated whole-virus preparation, an S1 spike-protein subunit (S1 antigen) and a receptor-binding domain (RBD antigen, amino acids 319–519) coated on lumazine synthase (LS) particles using SpyCather/SpyTag technology. The RBD antigen proved to be the most efficient immunogen, and the resulting chicken IgY antibodies derived from serum or yolk, displayed strong reactivity with ELISA and indirect immunofluorescence and broad neutralizing activity against SARS-CoV-2 variants, including Omicron BA.1 and BA.5. Preliminary in vivo studies using RBD–lumazine synthase yolk preparations in a hamster model showed that local application was well tolerated and not harmful. However, despite the in vitro neutralizing capacity, this antibody preparation did not show protective effect. Further studies on galenic properties seem to be necessary. The RBD–lumazine antigen proved to be suitable for producing SARS-CoV-2 specific antibodies that can be applied to such therapeutic approaches and as reference reagents for SARS-CoV-2 diagnostics, including virus neutralization assays.