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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.

Fluoroquinolones (FQs) are among the antibiotics whose widespread use in farm-raised animals results in potentially harmful residues in the end products. Additionally, most Thai farmers use antibiotics. Amoxicillin and enrofloxacin were commonly used by pig farms, and hens were given enrofloxacin to prevent immunization side effects. Moreover, antibiotic overuse has harmed food safety in the long term, and the use of low-dose antibiotics causes bacterial resistance. Herein, an indirect competitive enzyme-linked immunosorbent assay (icELISA) was used to make a fast, easy, sensitive, and cost-effective method for monitoring FQs residues. After immunizing hens with mixed multi-hapten ciprofloxacin-bovine serum albumin (CPFX-BSA) with norfloxacin-bovine serum albumin (NFX-BSA), the IgY antibody purified from egg yolk was used for the detection of FQs residues in chicken and pork samples. The efficiency of the IgY antibody showed excellent sensitivity, with 50% inhibitory concentration (IC50) of enrofloxacin at 0.05 µg/mL, far below the MRLs defined by the EU for muscle samples, which was not to exceed 100 µg/kg. The recovery range for chicken muscle samples spiked with ENFX concentrations of 1.00–0.01 µg/mL was 86.65–112.71%, similar to pork samples, which were 84.24–117.22.2%. This method has a lot of potential for analyzing fluoroquinolones in complex samples quickly, easily, and at a low cost on-site. The IgY-based ic ELISA was developed to detect ciprofloxacin (CPFX), norfloxacin (NFX), and enrofloxacin (ENFX) residues; it confirms that IgY could be a promising choice for the detection of antibiotic residues in food samples.

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.

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.

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. 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.

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.

Beak and feather disease virus (BFDV), a single-stranded DNA virus, infects endangered psittacine species, including the South African Cape parrot. The disease is highly contagious and can be transmitted through contact with contaminated faeces, crop secretions, and feather and skin dander. To date, there is no vaccine or cure available for BFDV. The production of an effective vaccine depends on having a production platform and methods that are both easy to use and capable of yielding a significant amount of protein that will induce a sufficient immune response. Therefore, the aim of this study was to produce a plant-based BFDV vaccine candidate and to evaluate its ability to elicit an immune response in birds. Recombinant BFDV capsid protein (CP) was transiently expressed in Nicotiana benthamiana and purified using density gradient ultracentrifugation. Japanese quails were immunized with purified BFDV CP. Yolk-derived IgY was purified by water dilution and salt precipitation, and its specificity was verified by western blot analysis. The expression levels of the coat protein increased from non-detectable to an average accumulation of 1.58 mg/kg of fresh plant tissue biomass, and antibodies against BFDV CP were detected in both the blood and eggs of immunized quails, indicating that vaccination with BFDV CP successfully elicited a humoral immune response. This study demonstrates that heterologous expression in plants is a viable method for producing BFDV CP. To the best of our knowledge, this is the first study to show the antibody response to a plant-produced BFDV antigen in a quail model. Given that the presence of anti-CP antibodies in infected birds is associated with immunity, this system can potentially be used to produce a vaccine against BFDV.

Inhalation allergies caused by cats and dogs can lead to a range of discomforting symptoms, such as rhinitis and asthma, in humans. With the increasing popularity of and care provided to these companion animals, the allergens they produce pose a growing threat to susceptible patients’ health. Allergens from cats and dogs have emerged as significant risk factors for triggering asthma and allergic rhinitis worldwide; however, there remains a lack of systematic measures aimed at assisting individuals in recognizing and preventing allergies caused by these animals. This review provides comprehensive insights into the classification of cat and dog allergens, along with their pathogenic mechanisms. This study also discusses implementation strategies for prevention and control measures, including physical methods, gene-editing technology, and immunological approaches, as well as potential strategies for enhancing allergen immunotherapy combined with immunoinformatics. Finally, it presents future prospects for the prevention and treatment of human allergies caused by cats and dogs. This review will improve knowledge regarding allergies to cats and dogs while providing insights into potential targets for the development of next-generation treatments.

Approximately 10–24% of people suffer from a cat allergy. Fel d 1, the major allergen, triggers reactions in approximately 94% of sensitized individuals. Current therapeutic strategies for allergic diseases primarily involve medication or immunotherapy to alleviate symptoms, which are often burdened by low efficacy, high cost, and extended duration, posing significant challenges for patients. In contrast, IgY antibodies offer a promising alternative by reducing the level of allergens produced by cats. In this study, T-cell epitopes of Fel d 1 were predicted using ProPred/CTLpred, connected via a suitable linker (GGGGS), and expressed in E. coli. Immunization of mice and hens with recombinant cFel d 1 yielded high-titer specific antibodies (IgG: 1:301,500; IgY: 1:4,194,304). Cats administered anti-cFel d 1 IgY-enriched yolk powder (1–3% of diet) for four weeks exhibited a 30–71% reduction in salivary Fel d 1. These findings indicate that the allergen epitope-targeted IgY strategy effectively reduces allergen levels in cats, providing a promising basis for preventing and treating allergic conditions.

The use of egg yolk antibodies—IgY technology—represents an alternative to the production of mammalian immunoglobulins and has several advantages regarding animal welfare and lower costs of production. The use of adjuvants to achieve the hyperimmunization of laying hens plays a key role in the success of the production of high levels of the antibodies. In the present work, two different adjuvant systems (Freund’s adjuvants and MontanideTM ISA 71 VG) were compared to produce IgY anti-Bothrops alternatus. For the first immunization, formalin-inactivated Salmonella was added to MontanideTM ISA 71 VG to emulate Freund’s complete adjuvant which includes a mycobacteria antigen. After eight immunizations, IgY produced by using either adjuvant was able to neutralize the lethal activity of the venom in a mouse model, but differences were found regarding the recognition of components of the venom between the two adjuvants tested. Overall, MontanideTM adjuvant used in this work could be a good alternative choice to produce antibodies capable of neutralizing the lethality of complex antigens. This adjuvant is commercially available and used in the formulation of several poultry vaccines and could be used for the IgY technology instead of traditional immunomodulators such as Freund’s adjuvants.Key points• IgY extracts recognized major components of the venom.• Avidity indexes of the IgY extracts increased after the successive immunizations.• IgY obtained by two adjuvant systems neutralized the lethal activity of the venom.