While variable regions of immunoglobulins are extensively diversified by V(D)J recombination and somatic hypermutation in vertebrates,the constant regions of immunoglobulin heavy chains also utilize certain mechanisms...While variable regions of immunoglobulins are extensively diversified by V(D)J recombination and somatic hypermutation in vertebrates,the constant regions of immunoglobulin heavy chains also utilize certain mechanisms to produce diversity,including class switch recombination(CSR),subclass differentiation,and alternative expression of the same gene.Many species of birds,reptiles,and amphibians express a truncated isoform of immunoglobulin Y(IgY),termed IgY(ΔFc),which lacks theυCH3 andυCH4 domains.In Anseriformes,IgY(ΔFc)arises from alternative transcriptional termination sites within the sameυgene,whereas in some turtles,intact IgY and IgY(ΔFc)are encoded by distinct genes.Different from the previously reported IgY(ΔFc)variants,this study identified a truncated IgY in the snake Elaphe taeniura,characterized by the loss of only a portion of the CH4 domain.Western blotting and liquid chromatographytandem mass spectrometry confirmed that this truncated IgY is generated by post-translational cleavage at N338 within the IgY heavy chain constant(CH)region.Furthermore,both human and snake asparaginyl endopeptidase were shown to cleave snake IgY in vitro.These findings reveal a novel mechanism for the production of shortened IgY forms,demonstrating that the immunoglobulin CH region undergoes diversification through distinct strategies across vertebrates.展开更多
The term“IgY technology”was introduced in the literature in the mid 1990s to describe a procedure involving immunization of avian species,mainly laying hens and consequent isolation of the polyclonal IgYs from the“...The term“IgY technology”was introduced in the literature in the mid 1990s to describe a procedure involving immunization of avian species,mainly laying hens and consequent isolation of the polyclonal IgYs from the“immune”egg yolk(thus avoiding bleeding and animal stress).IgYs have been applied to various fields of medicine and biotechnology.The present article will deal with specific aspects of IgY technology,focusing on the currently reported methods for developing,isolating,evaluating and storing polyclonal IgYs.Other topics such as current information on isolation protocols or evaluation of IgYs from different avian species are also discussed.Specific advantages of IgY technology(e.g.,novel antibody specificities that may emerge via the avian immune system)will also be discussed.Recent in vitro applications of polyclonal egg yolk-derived IgYs to the field of disease diagnosis in human and veterinary medicine through in vitro immunodetection of target biomolecules will be presented.Moreover,ethical aspects associated with animal well-being as well as new promising approaches that are relevant to the original IgY technology(e.g.,development of monoclonal IgYs and IgY-like antibodies through the phage display technique or in transgenic chickens)and future prospects in the area will also be mentioned.展开更多
基金supported by the Fundamental Research Funds for the Central Universities,Southwest Minzu University(ZYN2023097)Scientific and Technological Innovation Team for Qinghai-Xizang Plateau Research in Southwest Minzu University(2024CXTD13)。
文摘While variable regions of immunoglobulins are extensively diversified by V(D)J recombination and somatic hypermutation in vertebrates,the constant regions of immunoglobulin heavy chains also utilize certain mechanisms to produce diversity,including class switch recombination(CSR),subclass differentiation,and alternative expression of the same gene.Many species of birds,reptiles,and amphibians express a truncated isoform of immunoglobulin Y(IgY),termed IgY(ΔFc),which lacks theυCH3 andυCH4 domains.In Anseriformes,IgY(ΔFc)arises from alternative transcriptional termination sites within the sameυgene,whereas in some turtles,intact IgY and IgY(ΔFc)are encoded by distinct genes.Different from the previously reported IgY(ΔFc)variants,this study identified a truncated IgY in the snake Elaphe taeniura,characterized by the loss of only a portion of the CH4 domain.Western blotting and liquid chromatographytandem mass spectrometry confirmed that this truncated IgY is generated by post-translational cleavage at N338 within the IgY heavy chain constant(CH)region.Furthermore,both human and snake asparaginyl endopeptidase were shown to cleave snake IgY in vitro.These findings reveal a novel mechanism for the production of shortened IgY forms,demonstrating that the immunoglobulin CH region undergoes diversification through distinct strategies across vertebrates.
文摘The term“IgY technology”was introduced in the literature in the mid 1990s to describe a procedure involving immunization of avian species,mainly laying hens and consequent isolation of the polyclonal IgYs from the“immune”egg yolk(thus avoiding bleeding and animal stress).IgYs have been applied to various fields of medicine and biotechnology.The present article will deal with specific aspects of IgY technology,focusing on the currently reported methods for developing,isolating,evaluating and storing polyclonal IgYs.Other topics such as current information on isolation protocols or evaluation of IgYs from different avian species are also discussed.Specific advantages of IgY technology(e.g.,novel antibody specificities that may emerge via the avian immune system)will also be discussed.Recent in vitro applications of polyclonal egg yolk-derived IgYs to the field of disease diagnosis in human and veterinary medicine through in vitro immunodetection of target biomolecules will be presented.Moreover,ethical aspects associated with animal well-being as well as new promising approaches that are relevant to the original IgY technology(e.g.,development of monoclonal IgYs and IgY-like antibodies through the phage display technique or in transgenic chickens)and future prospects in the area will also be mentioned.
