Identification of the amino acid residues involved in human IgG transport into egg yolks of Japanese quail (Coturnix japonica)

Bae, Hae-duck; Kobayashi, Misato; Horio, Fumihiko; Murai, Atsushi

doi:10.1016/j.molimm.2010.02.011

Cited by 8 publications

(3 citation statements)

References 23 publications

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“…A simultaneous mutation of residues 252-254 (from MIS to GGG) located on the Cγ2 domain abolished IgG uptake into the egg yolks. We further expanded target amino acid residues for alanine and glycine-scanning mutagenesis on 16 amino acid residues located along the Cγ2/Cγ3 interface (Bae et al, 2010b). Wild-type human IgG1-Fc Journal of Poultry Science, 50 (3) (WT) and its mutants were synthesized, and their uptakes into the egg yolks of quail were determined.…”

Section: Studies Using Recombinant Ig and Site-directed Mutagenesis Tmentioning

confidence: 99%

Maternal Transfer of Immunoglobulins into Egg Yolks of Birds

Murai

2013

J. Poult. Sci.

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In avian species, maternal IgY transferred across egg yolks from mother to offspring plays a key role to protect the hatching chicks against pathogenic attacks. The process of avian maternal IgY transfer is divided into two steps: the first step is the transfer from the maternal circulation to the egg yolks of developing oocytes in the maternal body, and the second step is the transfer from the egg yolks to the embryonic circulation in the developing eggs. The second step relies on IgY-Fc receptor, FcRY, expressing on the yolk sac membrane. However, in the first step, the molecular basis of IgY transfer is still unknown. This review focused on the structural requirements of IgY and heterologous immunoglobulin such as human IgG for transferring into egg yolks of birds, and a plausible molecular mechanism for immunoglobulin uptake in ovarian follicles were discussed. Recent research revealed existence of a selective IgY transfer system that recognizes Cυ3/Cυ4 interface of IgY in ovarian follicles of birds.

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Section: Studies Using Recombinant Ig and Site-directed Mutagenesis Tmentioning

confidence: 99%

Maternal Transfer of Immunoglobulins into Egg Yolks of Birds

Murai

2013

J. Poult. Sci.

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“…Analysis of the FcRY/IgY complex structure by cryoelectron microscopy showed that FcRY is in close contact with IgY Cυ4 domain and its surroundings ( 11 ). The LYI (362–364 at Cυ3) and HEAL motif (550–553 at Cυ4) within the interface of Cυ3 and Cυ4 domain are conserved well in transportable Igs into egg yolks ( 20 , 21 ). The substitution of one amino acid residue in the region to other amino acids markedly impacts the uptake of mutants into egg yolks ( 7 , 8 ).…”

Section: Discussionmentioning

confidence: 99%

FcRY is a key molecule controlling maternal blood IgY transfer to yolks during egg development in avian species

Okamoto,

Sasaki,

Ikeda

et al. 2024

Front. Immunol.

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Maternal immunoglobulin transfer plays a key role in conferring passive immunity to neonates. Maternal blood immunoglobulin Y (IgY) in avian species is transported to newly-hatched chicks in two steps: 1) IgY is transported from the maternal circulation to the yolk of maturing oocytes, 2) the IgY deposited in yolk is transported to the circulation of the embryo via the yolk sac membrane. An IgY-Fc receptor, FcRY, is involved in the second step, but the mechanism of the first step is still unclear. We determined whether FcRY was also the basis for maternal blood IgY transfer to the yolk in the first step during egg development. Immunohistochemistry revealed that FcRY was expressed in the capillary endothelial cells in the internal theca layer of the ovarian follicle. Substitution of the amino acid residue in Fc region of IgY substantially changed the transport efficiency of IgY into egg yolks when intravenously-injected into laying quail; the G365A mutant had a high transport efficiency, but the Y363A mutant lacked transport ability. Binding analyses of IgY mutants to FcRY indicated that the mutant with a high transport efficiency (G365A) had a strong binding activity to FcRY; the mutants with a low transport efficiency (G365D, N408A) had a weak binding activity to FcRY. One exception, the Y363A mutant had a remarkably strong binding affinity to FcRY, with a small dissociation rate. The injection of neutralizing FcRY antibodies in laying quail markedly reduced IgY uptake into egg yolks. The neutralization also showed that FcRY was engaged in prolongation of half-life of IgY in the blood; FcRY is therefore a multifunctional receptor that controls avian immunity. The pattern of the transport of the IgY mutants from the maternal blood to the egg yolk was found to be identical to that from the fertilized egg yolk to the newly-hatched chick blood circulation, via the yolk sac membrane. FcRY is therefore a critical IgY receptor that regulates the IgY uptake from the maternal blood circulation into the yolk of avian species, further indicating that the two steps of maternal–newly-hatched IgY transfer are controlled by a single receptor.

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“…Our previous study showed that an Fc portion mainly containing C 3 and C 4 domains is essential for effective IgY transport into egg yolks, since intravenouslyinjected IgY-Fc fragments were effectively transported into egg yolks, whereas Fab and F(ab')2 fragments were poorly transported into egg yolks (Kitaguchi et al, 2008). It has been assumed that this selective IgY transport is mediated by an IgY-Fc receptor located on the perivitelline and/or oocyte plasma membrane (Morrison et al, 2001;Bae et al, 2010b;Kitaguchi et al, 2010), but such a receptor has not been identified yet, and the molecular basis of this selective IgY transport remains unclear.…”

Section: Introductionmentioning

confidence: 99%