Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa

Reproduction is fundamental to breeding programs aimed at increasing productivity in swine industry. However, the application of in vitro embryo production in this species is limited because of the polyspermy. Therefore, characterizing proteins involved in sperm-oocyte binding such as IZUMO1 becomes...

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Main Authors: Miranda Hernández-Falcó, Paula Sáez-Espinosa, Andrea López-Botella, Laura Robles-Gómez, Francisco Alberto García-Vázquez, Maria José Izquierdo-Rico, Pedro José Llamas-López, María José Gómez-Torres
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Language:English
Published: Frontiers Media S.A. 2025-05-01
Series:Frontiers in Cell and Developmental Biology
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Online Access:https://www.frontiersin.org/articles/10.3389/fcell.2025.1576881/full
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author Miranda Hernández-Falcó
Paula Sáez-Espinosa
Andrea López-Botella
Laura Robles-Gómez
Francisco Alberto García-Vázquez
Francisco Alberto García-Vázquez
Maria José Izquierdo-Rico
Maria José Izquierdo-Rico
Pedro José Llamas-López
María José Gómez-Torres
María José Gómez-Torres
author_facet Miranda Hernández-Falcó
Paula Sáez-Espinosa
Andrea López-Botella
Laura Robles-Gómez
Francisco Alberto García-Vázquez
Francisco Alberto García-Vázquez
Maria José Izquierdo-Rico
Maria José Izquierdo-Rico
Pedro José Llamas-López
María José Gómez-Torres
María José Gómez-Torres
author_sort Miranda Hernández-Falcó
collection DOAJ
description Reproduction is fundamental to breeding programs aimed at increasing productivity in swine industry. However, the application of in vitro embryo production in this species is limited because of the polyspermy. Therefore, characterizing proteins involved in sperm-oocyte binding such as IZUMO1 becomes essential. This study aimed to characterize porcine IZUMO1 protein under three different physiological states: sperm-rich fraction (SRF), 1-h capacitated sperm selected by swim-up (CS), and induced acrosome reaction in 1-h capacitated sperm (ARS). The immunolocalization of IZUMO1 and acrosome status of fifteen fertile boars was assessed by confocal microscopy. Additionally, six males were subjected to a more detailed examination via quantitative proteomic analysis by LC–MS/MS. Fluorescence results revealed four distinct IZUMO1 distribution patterns: pattern 1 (P1) characterized by speckled staining in the pre-equatorial subdomain and postacrosomal domain, pattern 2 (P2) displaying strong apical ridge staining with speckled staining in the pre-equatorial subdomain and postacrosomal domain, pattern 3 (P3) exhibiting speckled staining in the postacrosomal domain, and pattern 4 (P4) without labelling. In the SRF sperm, IZUMO1 was predominantly distributed between staining patterns P1 and P2 (∼50%). As a result of the capacitation, there was a significant decrease in P1. Conversely, in ARS, IZUMO1 was dominantly distributed in P3 51.55% and P4 24.25%. The quantitative study of the IZUMO1 protein supported these findings. With those results and compared with our previous work in human, here we propose a working model of IZUMO1 migration dependent on the morphology and subdomains of the sperm head.
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spelling doaj-art-1d2693ec81c04445a8029263a6694ea52025-08-20T03:08:16ZengFrontiers Media S.A.Frontiers in Cell and Developmental Biology2296-634X2025-05-011310.3389/fcell.2025.15768811576881Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoaMiranda Hernández-Falcó0Paula Sáez-Espinosa1Andrea López-Botella2Laura Robles-Gómez3Francisco Alberto García-Vázquez4Francisco Alberto García-Vázquez5Maria José Izquierdo-Rico6Maria José Izquierdo-Rico7Pedro José Llamas-López8María José Gómez-Torres9María José Gómez-Torres10Department of Biotechnology, University of Alicante, Alicante, SpainDepartment of Biotechnology, University of Alicante, Alicante, SpainDepartment of Biotechnology, University of Alicante, Alicante, SpainDepartment of Biotechnology, University of Alicante, Alicante, SpainDepartamento de Fisiología, Facultad de Veterinaria, Universidad de Murcia, Murcia, SpainInstituto Murciano de Investigación Biosanitaria (IMIB-Pascual Parrilla), Murcia, SpainInstituto Murciano de Investigación Biosanitaria (IMIB-Pascual Parrilla), Murcia, SpainDepartamento de Biología Celular e Histología, Facultad de Medicina, Universidad de Murcia, Murcia, SpainDepartment of Agri-Food Technology, University of Miguel Hernández, Elche, SpainDepartment of Biotechnology, University of Alicante, Alicante, SpainHuman Fertility Cathedra, University of Alicante, Alicante, SpainReproduction is fundamental to breeding programs aimed at increasing productivity in swine industry. However, the application of in vitro embryo production in this species is limited because of the polyspermy. Therefore, characterizing proteins involved in sperm-oocyte binding such as IZUMO1 becomes essential. This study aimed to characterize porcine IZUMO1 protein under three different physiological states: sperm-rich fraction (SRF), 1-h capacitated sperm selected by swim-up (CS), and induced acrosome reaction in 1-h capacitated sperm (ARS). The immunolocalization of IZUMO1 and acrosome status of fifteen fertile boars was assessed by confocal microscopy. Additionally, six males were subjected to a more detailed examination via quantitative proteomic analysis by LC–MS/MS. Fluorescence results revealed four distinct IZUMO1 distribution patterns: pattern 1 (P1) characterized by speckled staining in the pre-equatorial subdomain and postacrosomal domain, pattern 2 (P2) displaying strong apical ridge staining with speckled staining in the pre-equatorial subdomain and postacrosomal domain, pattern 3 (P3) exhibiting speckled staining in the postacrosomal domain, and pattern 4 (P4) without labelling. In the SRF sperm, IZUMO1 was predominantly distributed between staining patterns P1 and P2 (∼50%). As a result of the capacitation, there was a significant decrease in P1. Conversely, in ARS, IZUMO1 was dominantly distributed in P3 51.55% and P4 24.25%. The quantitative study of the IZUMO1 protein supported these findings. With those results and compared with our previous work in human, here we propose a working model of IZUMO1 migration dependent on the morphology and subdomains of the sperm head.https://www.frontiersin.org/articles/10.3389/fcell.2025.1576881/fullacrosome reactionboarcapacitationimmunofluorescenceIZUMO1proteomics
spellingShingle Miranda Hernández-Falcó
Paula Sáez-Espinosa
Andrea López-Botella
Laura Robles-Gómez
Francisco Alberto García-Vázquez
Francisco Alberto García-Vázquez
Maria José Izquierdo-Rico
Maria José Izquierdo-Rico
Pedro José Llamas-López
María José Gómez-Torres
María José Gómez-Torres
Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa
Frontiers in Cell and Developmental Biology
acrosome reaction
boar
capacitation
immunofluorescence
IZUMO1
proteomics
title Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa
title_full Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa
title_fullStr Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa
title_full_unstemmed Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa
title_short Immunolocalization and proteomic analyses of IZUMO1 in porcine spermatozoa
title_sort immunolocalization and proteomic analyses of izumo1 in porcine spermatozoa
topic acrosome reaction
boar
capacitation
immunofluorescence
IZUMO1
proteomics
url https://www.frontiersin.org/articles/10.3389/fcell.2025.1576881/full
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