Amino acid substitution in the Cυ3 domain causes either elevation or reduction of IgY uptake into egg yolks of quail

Takimoto, Takuou; Doi, Kasumi; Kobayashi, Misato; Horio, Fumihiko; Murai, Atsushi

doi:10.1016/j.vetimm.2013.03.011

Cited by 4 publications

(6 citation statements)

References 16 publications

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“…Y363A showed a similar inhibition activity to WT, whereas G365A more effectively inhibited the DIG-IgY binding to FcRY than WT. G365S, which has similar ability to transport IgY into egg yolks as G365A ( 8 ), also strongly inhibited the binding of DIG-IgY ( Figure 4D ). G365D and N408A, which are not usually transported to egg yolks ( 8 ), were substantially less potent in inhibiting DIG-IgY binding than the WT.…”

Section: Resultsmentioning

confidence: 90%

“…G365S, which has similar ability to transport IgY into egg yolks as G365A ( 8 ), also strongly inhibited the binding of DIG-IgY ( Figure 4D ). G365D and N408A, which are not usually transported to egg yolks ( 8 ), were substantially less potent in inhibiting DIG-IgY binding than the WT. These results indicate that the binding activity of IgY-Fc mutants to FcRY was consistent with the transport pattern of these mutants to egg yolks.…”

Section: Resultsmentioning

confidence: 90%

“…Recombinant IgY-Fc and its mutants can be used to clarify whether the IgY/FcRY interaction controls maternal IgY transfer. IgY-Fc mutants substituting one amino acid residue for alanine were generated in a previous study and have variable abilities for transport into yolks when injected into laying birds ( 8 ). Analysis of the transport efficiency and binding properties of IgY-Fc mutants can elucidate the involvement of FcRY in maternal IgY transfer.…”

Section: Resultsmentioning

confidence: 99%

“…The cDNA encoding the quail IgY (qIgY) υ-heavy chain was isolated from a quail splenocyte cDNA library ( 8 ). The gene encoding the Fc regions (H chain residues at 231–568) was isolated by polymerase chain reaction (PCR) from the template cDNA, and the PCR product was ligated into the Kpn I- Xho I cloning site of pSecTag2, a mammalian expression vector (Invitrogen, Carlsbad, CA), with a C-terminal 6 × His tag.…”

Section: Methodsmentioning

confidence: 99%

“…Intravenously-injected IgY and its Fc fragments are incorporated into egg yolks of laying hens more than Fab and F(ab’) fragments ( 6 ). Additionally, IgY-Fc mutants with an amino acid residue substituted at the interface of the Cυ3–Cυ4 domain produce large differences in uptake into the egg yolk ( 7 , 8 ). These results indicate that a receptor, which recognizes specific regions of the IgY-Fc domain, is involved in the first step of maternal IgY transfer.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 90%

Section: Resultsmentioning

confidence: 90%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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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Evaluation of a receptor gene responsible for maternal blood IgY transfer into egg yolks using bursectomized IgY-depleted chickens

et al. 2020

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In avian species, maternal immunoglobulin Y ( IgY ) is transferred from the blood to the yolks of maturing oocytes; however, the mechanism underlying this transfer is unknown. To gain insight into the mechanisms of maternal IgY transfer into egg yolks, IgY-depleted chickens were generated by removing the bursa of Fabricius (bursectomy) during egg incubation, and their egg production and IgY transport ability into egg yolks were determined. After hatching, blood IgY concentrations of the bursectomized chickens decreased gradually until sexual maturity, whereas those of IgA remained low from an early stage of growth (from at least 2 wk of age). Chickens identified as depleted in IgY through screening of blood IgY and IgA concentrations were raised to sexual maturity. At 20 wk of age, both blood and egg yolk IgY concentrations in the IgY-depleted group were 600-fold lower than those of the control group, whereas egg production did not differ between the groups. Intravenously injected, digoxigenin-labeled IgY uptake into the egg yolk was approximately 2-fold higher in the IgY-depleted chickens than in the controls, suggesting that IgY depletion may enhance IgY uptake in maturing oocytes. DNA microarray analysis of the germinal disc, including the oocyte nucleus, revealed that the expression levels of 73 genes were upregulated more than 1.5-fold in the IgY-depleted group, although we could not identify a convincing candidate gene for the IgY receptor. In conclusion, we successfully raised IgY-depleted chickens presenting a marked reduction in egg yolk IgY. The enhanced uptake of injected IgY into the egg yolks of the IgY-depleted chickens supports the existence of a selective IgY transport mechanism in maturing oocytes and ovarian follicles in avian species.

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An ELISA for quantifying quail IgY and characterizing maternal IgY transfer to egg yolk in several quail strains

Murai

Kakiuchi

Hamano

et al. 2016

Veterinary Immunology and Immunopathology

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Amino acid substitution in the Cυ3 domain causes either elevation or reduction of IgY uptake into egg yolks of quail

Cited by 4 publications

References 16 publications

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

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

Evaluation of a receptor gene responsible for maternal blood IgY transfer into egg yolks using bursectomized IgY-depleted chickens

An ELISA for quantifying quail IgY and characterizing maternal IgY transfer to egg yolk in several quail strains

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