Oviductin sets the species-specificity of the mammalian zona pellucida DOI Open Access

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

et al.

Published: Oct. 31, 2024

The zona pellucida (ZP) is vital for species-specific fertilization as this barrier mediates sperm-oocyte binding. Here, we determined whether sperm from distant mammalian orders (Carnivora, Primates, and Rodentia) could penetrate bovine oocytes by examining the role of oviductal fluid glycoprotein (OVGP1 or oviductin) bovine, murine, human sources in modulating species-specificity murine oocytes. Sperm all species were found to intact ovarian form hybrid embryos. However, contact with OVGP1, conferred ZP species-specificity, allowing only penetration corresponding regardless ZP’s origin. Glycolytic microstructural analyses revealed that OVGP1 covers pores present glycosylation determines specificity. This suggests specific capacity acquired oviduct through incorporation oviductin.

Language: Английский

Oviductin sets the species-specificity of the mammalian zona pellucida DOI Open Access

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

et al.

Published: Feb. 7, 2025

The zona pellucida (ZP) is vital for species-specific fertilization as this barrier mediates sperm-oocyte binding. Here, we determined whether sperm from distant mammalian orders (Carnivora, Primates, and Rodentia) could penetrate bovine oocytes by examining the role of oviductal fluid glycoprotein (OVGP1 or oviductin) bovine, murine, human sources in modulating species-specificity murine oocytes. Sperm all species were found to intact ovarian form hybrid embryos. However, contact with OVGP1, conferred ZP species-specificity, allowing only penetration corresponding regardless ZP’s origin. Glycolytic microstructural analyses revealed that OVGP1 covers pores present glycosylation determines specificity. This suggests specific capacity acquired oviduct through incorporation oviductin.

Language: Английский

Citations

0
Oviductin sets the species-specificity of the mammalian zona pellucida DOI Open Access

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

et al.

Published: March 27, 2025

The zona pellucida (ZP) is vital for species-specific fertilization as this barrier mediates sperm-oocyte binding. Here, we determined whether sperm from distant mammalian orders (Carnivora, Primates, and Rodentia) could penetrate bovine oocytes by examining the role of oviductal fluid glycoprotein (OVGP1 or oviductin) bovine, murine, human sources in modulating species-specificity murine oocytes. Sperm all species were found to intact ovarian form hybrid embryos. However, contact with OVGP1, conferred ZP species-specificity, allowing only penetration corresponding regardless ZP’s origin. Glycolytic microstructural analyses revealed that OVGP1 covers pores present glycosylation determines specificity. This suggests specific capacity acquired oviduct through incorporation oviductin.

Language: Английский

Citations

0
Oviductin sets the species-specificity of the mammalian zona pellucida DOI

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

et al.

bioRxiv (Cold Spring Harbor Laboratory), Journal Year: 2024, Volume and Issue: unknown

Published: July 3, 2024

Abstract The zona pellucida (ZP) is vital for species-specific fertilization as this barrier mediates sperm-oocyte binding. Here, we determined whether sperm from distant mammalian orders (Carnivora, Primates, and Rodentia) could penetrate bovine oocytes by examining the role of oviductal fluid glycoprotein (OVGP1 or oviductin) bovine, murine, human sources in modulating species-specificity murine oocytes. Sperm all species were found to intact ovarian form hybrid embryos. However, contact with OVGP1, conferred ZP species-specificity, allowing only penetration corresponding regardless ZP’s origin. Glycolytic microstructural analyses revealed that OVGP1 covers pores present glycosylation determines specificity. This suggests specific capacity acquired oviduct through incorporation oviductin. Teaser oocyte needs interact an protein called ensure same can fertilize egg.

Language: Английский

Citations

0
Oviductin sets the species-specificity of the mammalian zona pellucida DOI Open Access

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

et al.

Published: Oct. 31, 2024

The zona pellucida (ZP) is vital for species-specific fertilization as this barrier mediates sperm-oocyte binding. Here, we determined whether sperm from distant mammalian orders (Carnivora, Primates, and Rodentia) could penetrate bovine oocytes by examining the role of oviductal fluid glycoprotein (OVGP1 or oviductin) bovine, murine, human sources in modulating species specificity murine oocytes. Sperm all were found to intact ovarian form hybrid embryos. However, contact with OVGP1, conferred ZP specificity, allowing only penetration corresponding regardless ZP’s origin. Glycolytic microstructural analyses revealed that OVGP1 covers pores present glycosylation determines specificity. This suggests specific capacity acquired oviduct through incorporation oviductin.

Language: Английский

Citations

0
Oviductin sets the species-specificity of the mammalian zona pellucida DOI Open Access

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

et al.

Published: Oct. 31, 2024

The zona pellucida (ZP) is vital for species-specific fertilization as this barrier mediates sperm-oocyte binding. Here, we determined whether sperm from distant mammalian orders (Carnivora, Primates, and Rodentia) could penetrate bovine oocytes by examining the role of oviductal fluid glycoprotein (OVGP1 or oviductin) bovine, murine, human sources in modulating species-specificity murine oocytes. Sperm all species were found to intact ovarian form hybrid embryos. However, contact with OVGP1, conferred ZP species-specificity, allowing only penetration corresponding regardless ZP’s origin. Glycolytic microstructural analyses revealed that OVGP1 covers pores present glycosylation determines specificity. This suggests specific capacity acquired oviduct through incorporation oviductin.

Language: Английский

Citations

0