Proteomic Changes Associated With Sperm Fertilizing Ability in Meat-Type Roosters.

chicken fertility proteomic semen sperm

Journal

Frontiers in cell and developmental biology
ISSN: 2296-634X
Titre abrégé: Front Cell Dev Biol
Pays: Switzerland
ID NLM: 101630250

Informations de publication

Date de publication:
2021
Historique:
received: 19 01 2021
accepted: 03 03 2021
entrez: 26 4 2021
pubmed: 27 4 2021
medline: 27 4 2021
Statut: epublish

Résumé

The molecular basis of male fertility remains unclear, especially in chickens, where decades of genetic selection increased male fertility variability as a side effect. As transcription and translation are highly limited in sperm, proteins are key molecules defining their functionality, making proteomic approaches one of the most adequate methods to investigate sperm capacity. In this context, it is interesting to combine complementary proteomic approaches to maximize the identification of proteins related to sperm-fertilizing ability. In the present study, we aimed at identifying proteins related to fertility in meat-type roosters, showing fertility variability. Fertile roosters (fertility rates higher than 70% after artificial insemination) differed from subfertile roosters (fertility rates lower than 40%) in their sperm mass motility. Fertile and subfertile sperm protein contents were compared using two complementary label-free quantitative proteomic methods: Intact Cell MALDI-TOF-Mass Spectrometry and GeLC-MS/MS. Combining the two strategies, 57 proteins were identified as differentially abundant. Most of them were described for the first time as differentially abundant according to fertility in this species. These proteins were involved in various molecular pathways including flagellum integrity and movement, mitochondrial functions, sperm maturation, and storage in female tract as well as oocyte-sperm interaction. Collectively, our data improved our understanding of chicken sperm biology by revealing new actors involved in the complexity of male fertility that depends on multiple cell functions to reach optimal rates. This explains the inability of reductionist

Identifiants

pubmed: 33898456
doi: 10.3389/fcell.2021.655866
pmc: PMC8063615
doi:

Types de publication

Journal Article

Langues

eng

Pagination

655866

Informations de copyright

Copyright © 2021 Vitorino Carvalho, Soler, Thélie, Grasseau, Cordeiro, Tomas, Teixeira-Gomes, Labas and Blesblois.

Déclaration de conflit d'intérêts

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

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Auteurs

Anaïs Vitorino Carvalho (A)

CNRS, INRAE, Université de Tours, IFCE, Nouzilly, France.

Laura Soler (L)

INRAE, ENVT, INP-Purpan, UPS, UMR Toxalim, Toulouse, France.

Aurore Thélie (A)

CNRS, INRAE, Université de Tours, IFCE, Nouzilly, France.

Isabelle Grasseau (I)

CNRS, INRAE, Université de Tours, IFCE, Nouzilly, France.

Luiz Cordeiro (L)

CNRS, INRAE, Université de Tours, IFCE, Nouzilly, France.

Daniel Tomas (D)

CNRS, INRAE, Université de Tours, IFCE, Nouzilly, France.
INRAE, ENVT, INP-Purpan, UPS, UMR Toxalim, Toulouse, France.
INRAE, Université de Tours, CHU de Tours, Plate-forme PIXANIM (Phénotypage par Imagerie in/ex vivo de l'Animal à la Molécule), Nouzilly, France.

Ana-Paula Teixeira-Gomes (AP)

INRAE, Université de Tours, CHU de Tours, Plate-forme PIXANIM (Phénotypage par Imagerie in/ex vivo de l'Animal à la Molécule), Nouzilly, France.
INRAE, ISP, Université de Tours, Nouzilly, France.

Valérie Labas (V)

CNRS, INRAE, Université de Tours, IFCE, Nouzilly, France.
INRAE, ENVT, INP-Purpan, UPS, UMR Toxalim, Toulouse, France.
INRAE, Université de Tours, CHU de Tours, Plate-forme PIXANIM (Phénotypage par Imagerie in/ex vivo de l'Animal à la Molécule), Nouzilly, France.

Elisabeth Blesblois (E)

CNRS, INRAE, Université de Tours, IFCE, Nouzilly, France.

Classifications MeSH