Search Results (44)

Valued for their nutritional content, eggs have recently gained attention as a versatile biomaterial owing to their biocompatibility, biodegradability, and unique structural and biochemical composition. This review highlights the biomedical potential of various egg components—eggshell, eggshell membrane, egg white, and egg yolk—and their applications in bone grafting, tissue engineering, wound healing, drug delivery, and biosensors. Eggshells serve as a natural, calcium-rich source for bone tissue engineering and regenerative medicine. The eggshell membrane, with its antimicrobial and structural properties, offers promise as a wound healing scaffold. Egg white, known for its gelation and film-forming capabilities, is utilized in hydrogel-based systems for drug delivery and biosensing. Egg yolk, rich in lipids and immunoglobulin Y (IgY) antibodies, is being explored for diagnostic and therapeutic applications. This review critically examines the advantages and limitations of each egg-derived component and outlines current research gaps, offering insights into future directions for the development of egg-based biomaterials in biomedical engineering. Full article

Egg yolk immunoglobulin Y (IgY) possesses advantages such as low cost, easy availability, simple preparation, high antigen specificity, absence of drug residues, and compliance with animal welfare standards, making it an environmentally friendly and safe alternative to antibiotics. This research utilizes IgY antibody technology to develop a multivalent passive immune vaccine for major pathogenic bacteria in aquaculture. In this study, IgY antibodies against live Shewanella xiamenensis (LSX-IgY) and inactivated S. xiamenensis (ISX-IgY) were prepared by immunizing laying hens, and passive immunization protection experiments were conducted in Carassius auratus infected with S. xiamenensis and Aeromonas hydrophila. The passive immunization protection rates of LSX-IgY and ISX-IgY against S. xiamenensis were 63.64% and 72.73%, respectively, and the passive cross-protection rates against A. hydrophila were 50% and 71.43%, respectively. Further, C. auratus sera could specifically bind to S. xiamenensis or A. hydrophila in vitro, and the phagocytic activity of leukocytes was increased. LSX-IgY and ISX-IgY could reduce the bacterial load in the C. auratus kidneys. Meanwhile, they could significantly reduce the levels of antioxidant factors in serum and inhibit the mRNA expression of inflammation-related factors in the kidneys and spleens. Additionally, histopathology and immunofluorescence analysis showed that both IgY preparations preserved tissue integrity and reduced the expression of apoptosis factor (p53) and DNA damage factor (γH2A.X) of visceral organs, respectively. In summary, LSX-IgY and ISX-IgY can combat various bacterial infections, with no significant difference between the two. Additionally, inactivated bacterial immunization is more aligned with animal welfare standards for laying hens. Therefore, ISX-IgY is expected to serve as a multivalent vaccine against major aquaculture pathogens. Full article

Tilapia lake virus (TiLV) poses a major threat to global tilapia aquaculture and contributes to significant economic losses due to the absence of effective vaccines and treatments. Given the high mortality rates and severe pathological effects of TiLV on tilapia, alternative strategies, such as immunoglobulin-based therapies, are being considered for disease control. In this study, we developed specific immunoglobulin Y (IgY) antibodies against TiLV and evaluated their neutralization activity. Laying hens were immunized via intramuscular injections of recombinant TiLV segment 4 protein, and IgY antibodies were extracted and purified from their egg yolks using polyethylene glycol precipitation. Western blot analysis confirmed the specificity of the IgY, which demonstrated no cross-reactivity with nontarget proteins. Neutralization assays revealed a dose-dependent reduction in TiLV infectivity, which declined from 5.01 × 10⁶ TCID₅₀/mL to 5.01 × 10⁴–1.26 × 10⁵ TCID₅₀/mL, with the highest efficacy observed at a 1:2 dilution. Despite the variability in neutralization infectivity among the different hens, IgY effectively inhibited TiLV-induced cytopathic effects. Immunofluorescence assays further confirmed a significant reduction in the TiLV antigen levels in IgY-treated RHTiB cells. Our findings highlight IgY as a promising strategy for TiLV control and suggest its potential application in the prevention of emerging viruses. Full article

Immunoglobulin Y (IgY) is the primary antibody found in the eggs of chicken (Gallus domesticus), allowing for large-scale antibody production with high titers, making them cost-effective antibody producers. IgY serves as a valuable alternative to mammalian antibodies typically used in immunodiagnostics and immunotherapy. Compared to mammalian antibodies, IgY offers several biochemical advantages, and its straightforward purification from egg yolk eliminates the need for invasive procedures like blood collection, reducing stress in animals. Due to the evolutionary differences between birds and mammals, chicken antibodies can bind to a broader range of epitopes on mammalian proteins than their mammalian counterparts. Studies have shown that chicken antibodies bind 3–5 times more effectively to rabbit IgG than swine antibodies, enhancing the signal in immunological assays. Additionally, IgY does not interact with rheumatoid factors or human anti-mouse IgG antibodies (HAMA), helping to minimize interference from these factors. IgY obtained from egg yolk of hens immunized against Pseudomonas aeruginosa has been used in patients suffering from cystic fibrosis and chronic pulmonary colonization with this bacterium. Furthermore, IgY has been used to counteract streptococcus mutans in the oral cavity and for the treatment of enteral infections in both humans and animals. However, the use of avian antibodies is limited to pulmonary, enteral, or topical application and should, due to immunogenicity, not be used for systemic administration. Thus, IgY expands the range of strategies available for combating pathogens in medicine, as a promising candidate both as an alternative to antibiotics and as a valuable tool in research and diagnostics. Full article

The overuse of antibiotics in animal husbandry has driven the search for alternative strategies to combat zoonotic pathogens. Foodborne zoonotic diseases caused by pathogenic bacteria pose a significant threat to human health, and therefore food safety should be a priority. This study investigates the in vitro inhibitory effects of chicken egg yolk immunoglobulin Y (IgY) on the growth and viability of three major foodborne pathogens: Campylobacter jejuni, Salmonella spp., and Escherichia coli. IgY was isolated from immunized hen egg yolks using a modified water dilution method, and its antigen-specificity confirmed through agglutination assays. Growth inhibition was evaluated across multiple doses and time points, revealing a dose-dependent bacteriostatic effect against all tested pathogens. A single dose of IgY (0.5 mg/mL) significantly reduced C. jejuni counts by up to 7 log, while repeated doses were required for Salmonella spp. and E. coli. These findings highlight egg yolk immunoglobulin’s potential as a source of sustainable, effective, ethical, readily available, and inexpensive antibiotic substitutes in livestock management. Future research will focus on validating these results in vivo and exploring large-scale production of IgY for practical application in animal healthcare. Full article

The objective of this experiment is to investigate the effects of SAP or SAO as ω-3 PUFA raw materials on production performance, egg quality, serum immunity, serum lipids, and fatty acid deposition patterns in the eggs of laying quails. Chinese yellow-feathered quails served as the experimental subjects. A single-factor design was employed to randomly assign 1288 quails into four treatment groups, with seven replicates per treatment and 46 birds in each replicate. The groups included a control group (basal diet with no SAP), 1.6% SAP, 3.2% SAP, and 0.8% SAP + 0.3% SAO. The results indicate that: (1) Compared to the control group, the 0.8% SAP + 0.3% SAO group exhibited a reduction in daily egg-laying rate and egg mass, alongside an increased FCR; (2) the 3.2% SAP group enhanced egg yolk color, while the 1.6% SAP group reduced eggshell thickness, and the 0.8% SAP + 0.3% SAO group increased eggshell thickness; (3) compared to the control group, the 3.2% SAP group decreased total cholesterol (TC) and high-density lipoprotein cholesterol (HDL-C) levels in serum; the addition of either the 3.2% SAP or the 0.8% SAP + 0.3% SAO group significantly elevated quail serum immunoglobulin M (IgM) levels (p < 0.05); (4) in comparison to the control group, the addition of SAP or with SAP increased the contents of monounsaturated fatty acids (MUFA), polyunsaturated fatty acids (PUFA), docosahexaenoic acid (DHA), and ω-3 PUFA in 56-day-old egg yolks while reducing the ω-6/ω-3 ratio (p < 0.05). These findings suggest that SAP as a source of ω-3 PUFA raw materials could improve quail health by improving lipid metabolism and immunity. 3.2% SAP was recommended as the optimal level to produce the enriched ω-3 PUFA quail eggs with the ω-3 PUFA ≥ 300 mg/100 g. Full article

Chicken yolk immunoglobulin (IgY) is a natural immunologically active antibody extracted from egg yolk and can be used as a natural dietary supplement for the treatment of inflammation and damage to the intestines. In our study, IgY was embedded in a double emulsion (W/O/W; DE) to explore the therapeutic effect of the embedded IgY on Lipopolysaccharide (LPS)-induced jejunal injury in mice. The results showed that W/O/W-embedded IgY as a dietary supplement (IgY + DE) attenuated LPS-induced damage to mouse small intestinal structures and protected the integrity of the jejunal mucosal barrier. IgY + DE increased the amount of related transcription factors (Math1, Spdef, Elf3, and Klf4) and promoted thrush cell differentiation. IgY + DE ameliorated LPS-induced reduction in mucin quantity and markers. It promoted the expression of Muc1 and Muc2 and increased the mRNA expression levels of Muc1, Muc2, Muc3, Muc4, Muc13, and Agr2 (p < 0.05). IgY + DE increased the expression of several glycosyltransferases involved in mucin glycosylation. IgY + DE also neutralized the LPS attack on the expression of jejunal inflammatory factors IL-1β, IL-6, IL-4, and TNF-α. In conclusion, the IgY-embedded double emulsion can be used as a dietary supplement for immunotherapy to prevent LPS-induced jejunal injury in mice. Full article

Benzo[a]pyrene (B[a]P) is a hazardous polycyclic aromatic hydrocarbon that accumulates in several environmental matrices as a result of incomplete combustion. Its presence, carcinogenic properties, and tendency for bioaccumulation provide significant risks to human health and the environment. The objective of this study is to create an immunoassay for the detection of benzo[a]pyrene utilizing immunoglobulin Y antibodies. An indirect competitive enzyme-linked immunosorbent assay (ic-ELISA) was utilized to develop a speedy, straightforward, sensitive, and economical approach for detecting B[a]P residues. Following the immunization of hens with the hapten pyrenebutyric acid-bovine serum albumin (PyBA-BSA), the IgY antibody extracted from egg yolk was utilized to identify B[a]P residues. To evaluate antibody specificity, six PAH derivatives—PyBA, B[a]P, Chrysene, Benzo[b]fluoranthene, Benzo[a]anthracene, and Benzo[k]fluoranthene—were examined in the experiment to compete for binding with PyBA. The findings indicate that the antibody had considerable affinity for Chrysene (1.15%), Benzo[b]fluoranthene (311.32%), Benzo[k]fluoranthene (10.62%), Benzo[a]anthracene (22.82%), and PyBA (9.55%). Nonetheless, its affinity for B[a]P remained at 100%. The recovery range for grilled pork samples spiked with B[a]P doses of 10.00–0.1 μg/mL was 74.99% to 143.11%. This study utilized a polyclonal antibody, employing the IgY antibody for the inaugural development of an immunoassay to detect benzo[a]pyrene. The ELISA had a higher IC₅₀ value compared to the other immunoassays; however, it yielded good results. This immunoassay signifies a substantial progression in environmental analytical chemistry, offering a cost-effective and accessible technique for the detection of B[a]P to protect human health and the environment. Full article

This study was conducted to investigate the effects of different levels of Green Tea Powder on the performance, egg quality, serum immune and antioxidant indices, and cecal microflora of 300-day-old Chishui black-bone chickens during the peak laying period. A total of 360 Chishui black-bone chickens were selected as the experimental animals. They were randomly allocated into four groups: the control group (CON), trial group I (T1), trial group II (T2), and trial group III (T3), each group with six replicates and 15 hens in each replicate. The control group was fed a basal diet, and the experimental groups were fed a basal diet supplemented with 0.8%, 1.6%, and 2.4% Green Tea Powder, respectively. The accommodation period was 14 d, and the experimental period was 60 d. The statistical software SPSS was used to perform a one-way analysis of variance (ANOVA) on the experimental data, and Duncan’s method was used to perform multiple comparisons among groups. The results showed the following: compared with those of the control group, the average daily gain of the laying hens significantly decreased in the 1.6% Green Tea Powder group (p < 0.05); adding Green Tea Powder significantly reduced the content of malondialdehyde in the serum (p < 0.05), and the addition of 0.8% tea leaves significantly increased the immunoglobulin M and immunoglobulin A contents (p < 0.05); the egg yolk weight, eggshell thickness, eggshell strength, and yolk color of the laying hens significantly decreased in the 1.6% Green Tea Powder group (p < 0.05), and the addition of Green Tea Powder at the level of 2.4% significantly increased the percentage of umami, essential, and total amino acids (p < 0.05); and the structure of intestinal microorganisms was improved, and the abundance of Bacteroidetes and Bacteroidaceae significantly increased, while the abundance of Firmicutes and Lachnospiraceae significantly decreased (p < 0.05). Full article

Chicken yolk immunoglobulin (IgY), an immunologically active component, is used as an alternative to antibiotics for the treatment of enteritis. In this study, IgY was embedded in a W/O/W emulsion to overcome the digestive barrier and to investigate the protective effect of IgY against LPS-induced enteritis in mice. Four different hydrophilic emulsifiers (T80, PC, SC, and WPI) were selected to prepare separate W/O/W emulsions for encapsulating IgY. The results showed that the IgY-embedded double emulsion in the WPI group was the most effective. IgY embedded in the W/O/W emulsion could reduce the damage of LPS to the mouse intestine and prevent LPS-induced intestinal mucosal damage in mice. It increased the number of cup cells, promoted the expression of Muc2, and increased the mRNA expression levels of KLF3, TFF3, Itln1, and Ang4 (p < 0.05). It also enhanced the antioxidant capacity of the colon tissue, reduced the level of inflammatory factors in the colon tissue, and protected the integrity of the colon tissue. Stable embedding of IgY could be achieved using the W/O/W emulsion. In addition, the IgY-embedded W/O/W emulsion can be used as a dietary supplement to protect against LPS-induced enteritis in mice. Full article

Immunoglobulins Y (IgY) purified from egg yolks of hens represents an attractive, cost-effective alternative for the development of new diagnostic and therapeutic platforms. In this study, we evaluated the therapeutic efficacy of rotavirus-specific IgY in a cynomolgus monkey (Macaca fascicularis) model. Animals were experimentally infected with human rotavirus Group A (RVA), the most common cause of severe acute diarrhoea among young children worldwide. Animals were administered human RVA (3.1 × 10⁷ FFU/mL) by oral gavage, challenged with 2.5 mg of anti-RVA IgY orally, and monitored for five days according to clinical, haematological and biochemical parameters; serum electrolyte levels; viral shedding; and histopathological changes. Immunotherapy with anti-RVA IgY had a protective effect against severe rotavirus-induced enteritis in four of the ten treated monkeys, as evidenced by histopathological findings. Although only one animal had diarrhoea, all but one exhibited virus shedding regardless of the treatment. Full article

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. Full article

The H9N2 avian influenza virus causes reduced production performance and immunosuppression in chickens. The chicken yolk sac immunoglobulins (IgY) receptor (FcRY) transports from the yolk into the embryo, providing offspring with passive immunity to infection against common poultry pathogens. FcRY is expressed in many tissues/organs of the chicken; however, there are no reports investigating FcRY expression in chicken macrophage cells, and how H9N2-infected HD11 cells (a chicken macrophage-like cell line) regulate FcRY expression remains uninvestigated. This study used the H9N2 virus as a model pathogen to explore the regulation of FcRY expression in avian macrophages. FcRY was highly expressed in HD11 cells, as shown by reverse transcription polymerase chain reactions, and indirect immunofluorescence indicated that FcRY was widely expressed in HD11 cells. HD11 cells infected with live H9N2 virus exhibited downregulated FcRY expression. Transfection of eukaryotic expression plasmids encoding each viral protein of H9N2 into HD11 cells revealed that nonstructural protein (NS1) and matrix protein (M1) downregulated FcRY expression. In addition, the use of a c-jun N-terminal kinase (JNK) activator inhibited the expression of FcRY, while a JNK inhibitor antagonized the downregulation of FcRY expression by live H9N2 virus, NS1 and M1 proteins. Finally, a dual luciferase reporter system showed that both the M1 protein and the transcription factor c-jun inhibited FcRY expression at the transcriptional level. Taken together, the transcription factor c-jun was a negative regulator of FcRY, while the live H9N2 virus, NS1, and M1 proteins downregulated the FcRY expression through activating the JNK signaling pathway. This provides an experimental basis for a novel mechanism of immunosuppression in the H9N2 avian influenza virus. Full article

Post-fermented tea (PFT) is one of the most commonly consumed beverages worldwide. Rapid microbial growth and significant changes in the microbial composition of PFT during processing and storage pose a potential risk of contamination with mycotoxins such as zearalenone (ZEN). Screening for ZEN contamination in a simple, rapid, and inexpensive manner is required to ensure that PFT is safe for consumption. To monitor ZEN in PFT, ZEN was conjugated with bovine serum albumin to prepare egg yolk immunoglobulins (IgY). A specific indirect competitive enzyme-linked immunosorbent assay (ic-ELISA) based on IgY was developed and validated. ZEN was extracted with acetonitrile and water (50:50, v/v) containing 5% acetic acid and purified using a mixture of primary and secondary amines and graphitized carbon black to remove matrix interference from the PFT samples. Under optimal conditions, the linear range of this assay was 13.8−508.9 ng mL⁻¹, the limit of detection was 9.3 ng mL⁻¹, and the half-maximal inhibitory concentration was 83.8 ng mL⁻¹. Cross-reactivity was negligible, and the assay was specific for ZEN-related molecules. The recovery rate of ZEN in the control blanks of PFT samples spiked with a defined concentration of ZEN of 89.5% to 98.0%. The recovery and accuracy of the method were qualified for PFT matrices. No significant differences were evident between the results of the actual PFT samples analyzed by high-performance liquid chromatography and ic-ELISA. The collective data indicate that the developed ic-ELISA can be used for the rapid and simple detection of ZEN in PFT products. Full article

The use of antimicrobial growth promoters (AGPs) is banned because of problems associated with drug residues in animal products and increased bacterial resistance. The immunization of chickens with specific antigens is a promising strategy for generating specific antibodies that can target a wide range of antibiotic-resistant bacteria and can be used as an alternative to antibiotics. Immunoglobulin Y (IgY) antibodies in a polyclonal antibody (pAb) format, when administered orally, modulate the ruminal microbiome and maintain animal health and performance; however, there are concerns pertaining to protein impurities and biotin concentrations in the samples. Signal amplification strategies involving the noncovalent interaction of biotin with streptavidin is extensively used in diagnosis and scientific research, particularly in enzyme-linked immunosorbent assays (ELISAs). However, the high concentrations of biotin in samples, especially in those derived from rich sources such as egg yolk, can pose challenges and potentially harm the accuracy of diagnostic tests and protein concentration measurements. This study aimed to evaluate the influence of biotin on the measurement of IgY in freeze-dried egg yolk samples obtained from immunized laying hens using immunoassays with biotin–avidin/streptavidin. The detection of IgY in yolk samples using ELISA with streptavidin–biotin binding could lead to misdiagnosis due to biotin interference; the level of interference varies with the specific assay conditions and the concentration of biotin in the yolk samples. An ELISA without streptavidin–biotin binding is advisable to avoid interactions between biotin and target proteins, prevent biotin interference with the results, and achieve more reliable and accurate results. Full article