{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T23:48:13Z","timestamp":1790725693317,"version":"4.1.0"},"reference-count":80,"publisher":"Public Library of Science (PLoS)","issue":"6","license":[{"start":{"date-parts":[[2021,6,4]],"date-time":"2021-06-04T00:00:00Z","timestamp":1622764800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","award":["RGPIN-2017-06386"],"award-info":[{"award-number":["RGPIN-2017-06386"]}],"id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Faculty of agriculture and food science, University Laval"},{"name":"Centre de recherche en reproduction, d\u00e9veloppement et sant\u00e9 interg\u00e9n\u00e9rationnelle"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"abstract":"<jats:p>In boar sperm, we have previously shown that capacitation is associated with the appearance of the p32 tyrosine phosphoprotein complex. The principal tyrosine phosphoprotein involved in this complex is the acrosin-binding protein (ACRBP), which regulates the autoconversion of proacrosin to intermediate forms of acrosin in both boar and mouse sperm. However, the complete biological role of ACRBP has not yet been elucidated. In this study, we tested the hypothesis that tyrosine phophorylation and the presence of the ACRBP in the sperm head are largely necessary to induce capacitation, the acrosome reaction (AR) and sperm-zona pellucida (ZP) binding, all of which are necessary steps for fertilization.<jats:italic>In vitro<\/jats:italic>fertilization (IVF) was performed using matured porcine oocytes and pre-capacitated boar sperm cultured with anti-phosphotyrosine antibodies or antibodies against ACRBP. Anti-ACRBP antibodies reduced capacitation and spontaneous AR (P&lt;0.05). Sperm-ZP binding declined in the presence of anti-phosphotyrosine or anti-ACRBP antibodies. The localisation of anti-ACRBP antibodies on the sperm head, reduced the ability of the sperm to undergo the AR in response to solubilized ZP or by inhibiting the sarco\/endoplasmic reticulum Ca<jats:sup>2+<\/jats:sup>-ATPase. These results support our hypothesis that tyrosine phosphorylated proteins and ACRBP are present upon the sperm surface in order to participate in sperm-ZP binding, and that ACRBP upon the surface of the sperm head facilitates capacitation and the AR in the porcine.<\/jats:p>","DOI":"10.1371\/journal.pone.0251973","type":"journal-article","created":{"date-parts":[[2021,6,4]],"date-time":"2021-06-04T17:26:38Z","timestamp":1622827598000},"page":"e0251973","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":23,"title":["ACRBP (Sp32) is involved in priming sperm for the acrosome reaction and the binding of sperm to the zona pellucida in a porcine model"],"prefix":"10.1371","volume":"16","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2412-4708","authenticated-orcid":true,"given":"Yoku","family":"Kato","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Satheesh","family":"Kumar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christian","family":"Lessard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Janice L.","family":"Bailey","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2021,6,4]]},"reference":[{"key":"pone.0251973.ref001","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1071\/BI9510581","article-title":"Observations on the penetration of the sperm into the mammalian egg","volume":"4","author":"C Austin","year":"1951","journal-title":"Aust J Biol Sci"},{"key":"pone.0251973.ref002","doi-asserted-by":"crossref","first-page":"697","DOI":"10.1038\/168697b0","article-title":"Fertilizing capacity of spermatozoa deposited into fallopian tubes","volume":"168","author":"M Chang","year":"1951","journal-title":"Nature"},{"key":"pone.0251973.ref003","first-page":"189","volume-title":"The Physiology of Reproduction","author":"R Yanagimachi","year":"1994"},{"key":"pone.0251973.ref004","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1095\/biolreprod59.6.1328","article-title":"Cyclodextrin removes cholesterol from mouse sperm and induces capacitation in a protein-free medium","volume":"59","author":"YH Choi","year":"1998","journal-title":"Biol Reprod"},{"key":"pone.0251973.ref005","doi-asserted-by":"crossref","first-page":"334","DOI":"10.3109\/19396368.2010.512377","article-title":"Factors regulating sperm capacitation","volume":"56","author":"JL Bailey","year":"2010","journal-title":"Syst Biol Reprod Med"},{"key":"pone.0251973.ref006","doi-asserted-by":"crossref","first-page":"e0129285","DOI":"10.1371\/journal.pone.0129285","article-title":"Changes in Sperm motility and capacitation induce chromosomal aberration of the bovine embryo following intracytoplasmic sperm injection","volume":"10","author":"Y Kato","year":"2015","journal-title":"PLOS One"},{"key":"pone.0251973.ref007","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1242\/dev.121.4.1139","article-title":"Capacitation of mouse spermatozoa. 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