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

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

и другие.

Опубликована: Окт. 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.

Язык: Английский

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

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

и другие.

Опубликована: Фев. 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.

Язык: Английский

Процитировано

0

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

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

и другие.

Опубликована: Март 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.

Язык: Английский

Процитировано

0

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

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

и другие.

bioRxiv (Cold Spring Harbor Laboratory), Год журнала: 2024, Номер unknown

Опубликована: Июль 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.

Язык: Английский

Процитировано

0

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

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

и другие.

Опубликована: Окт. 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.

Язык: Английский

Процитировано

0

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

Daniel de la Fuente,

María Maroto, Yulia N. Cajas

и другие.

Опубликована: Окт. 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.

Язык: Английский

Процитировано

0