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The main immunoglobulin (IgY) present in avian blood presents some advantages over mammalian serum immunoglobulins regarding productivity, animal welfare and specificity. Moreover, due to structural differences and phylogenetic distance, IgY is more suitable for diagnostic purposes than mammalian antibodies, since it does not react with certain components of the human immune system and displays greater avidity for mammalian conserved proteins. IgY has been extensively used in health researches, as both a therapeutic and diagnostic tool.
Viral Infections Diagnosis
The ability of IgY to detect viral pathogens of the gastrointestinal tract in humans and animals has been widely studied. For example, IgY raised against canine parvovirus viral-like particles were used in ELISA and immunochromatography, showing sensitivity and specificity in the detection of canine parvovirus in dog fecal samples. Da Silva et al. (Silva, 2012) used IgY against hepatitis A virus (HAV) in a competitive immunoenzymatic assay to detect anti-HAV IgG in serum samples, showing satisfactory sensitivity and specificity. More recently, IgY against HAV was used to detect the virus in hepatic sections of infected rhesus monkeys by means of indirect immunofluorescence. Anti-HVA IgY was more efficient than the commercially available IgG for the detection of the same antigen.
Bacterial Infections Diagnosis
One of the most studied diagnostic potentials of IgY is against Staphylococcus aureus. The fact that the Fc portion of IgG reacts with the staphylococcal protein A makes IgY a relevant resource for more specific detection of different Staphylococcus aureus strains and their toxins since the Fc portion of IgY does not react with protein A. Following this rationale, Walczak et al. (Walczak, 2015) produced IgY against the fibrinogen binding protein (Efb) of Staphylococcus aureus and against a peptide epitope that encompasses the residues of Efb protein. Anti-Efb and anti-Efb antibodies presented high titers in ELISA and strong avidity in Western blot, showing promising use in the diagnosis of Staphylococcus aureus infection.
Parasitic Infections Diagnosis
Among the parasitic infections tested, previous studies have evaluated the potential of IgY in detecting the protozoan Toxoplasma gondii by producing IgY against its surface protein, which reacted with the target antigen in ELISA and Western blot. Therefore, revealing a potential diagnostic test for toxoplasmosis. IgY conjugated to fluorescein isothiocyanate has detected T. gondii tachyzoites in a colony, by means of immunofluorescence, and may be used to detect the protozoan in other types of samples.
Diagnosis of Tumors
Several researchers have been investigating the potential of IgY in the detection of tumor markers. IgY against the peptide antigen CA 15-3, a commonly used breast cancer marker, was used as secondary antibody in a sandwich ELISA aiming to detect CA 15-3, showing potential for clinical use. Sun et al. (Sun, 2015) produced IgY against two portions of the transmembrane glycoprotein HER2, which effectively detected the HER2 glycoprotein in cultured breast cancer cells by immunofluorescence and in sections of breast tumors overexpressing HER2, using immunohistochemistry. In addition, the antibodies bound to the glycoprotein in ELISA and Western blot, which indicate that IgY against HER2 is promising for use in breast cancer diagnosis.
Hematological Tests
Hens immunized with umbilical cord sera produced specific IgY against IgG and the complement fractions C3b and C3d. These antibodies did not react with the C4b fraction - which configures a higher specificity since anti-C4b antibodies often cross-reacts with the antigens of Chido/Rodgers RBC group - nor with erythrocyte antigens from ABO group. These antibodies are, therefore, promising as a reagent for Coombs test.
Enzyme Detection
IgY immunoassays were used to detect the hepatic expression of Cytochrome P450 2E1 (CYP2E1) in mice treated with medicinal herbs and products derived from plants rich in flavonoids. CYP2E1 metabolizes a wide variety of chemicals with different structures, in particular small and hydrophobic compounds, including potential cytotoxic and carcinogenic agents. Anti-CYP2E1 IgY was specific, without reacting with other cytochromes, and was able to detect the reduction of hepatic CYPE2E1 expression due to the ingestion of natural products with hepatoprotective effects.
Identification of Substances
The ability of IgY in identifying harmful substances in consumer products has been evaluated. An ELISA test was developed to detect the staphylococcal enterotoxin G (SEG), using specific IgY, and showed satisfactory sensitivity and specificity, reducing the interference of protein A that occurs in IgG tests. This test was successfully used to detect SEG in milk and dairy products samples and could therefore be used to identify the toxin in food. IgY can also be used in assays to identify antibiotic residues in food products of animal origin. Anti-gentamycin IgY can specifically detect the target antibiotic present in animal origin products. Following this rationale, researchers used specific IgY to detect kanamycin and gentamycin residues in milk and meat samples through competition ELISA and fluorescence polarization immunoassay.
Fig 1. Structural of chicken egg yolk antibody (IgY) and its recombinant scFv fragment structures. (Somasundaram, 2020)
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References
- Silva, A., et al. An immunoenzymatic assay for the diagnosis of hepatitis A utilising immunoglobulin Y. Memorias do Instituto Oswaldo Cruz. 2012, 107(7): 960–963.
- Walczak, et al. Method for generation of peptide-specific IgY antibodies directed to Staphylococcus aureus extracellular fibrinogen binding protein epitope. Biopolymers. 2015, 104(5): 552–559.
- Sun, Y., et al. Highly sensitive detection of cancer antigen human epidermal growth factor receptor 2 using novel chicken egg yolk immunoglobulin. Biologicals: journal of the International Association of Biological Standardization. 2015, 43(3): 165–170.
- Somasundaram, R., et al. An approach towards development of monoclonal IgY antibodies against SARS CoV-2 spike protein (S) using phage display method: A review. International immunopharmacology. 2020, 85, 106654.
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