Sperm Proteome after Interaction with Reproductive Fluids in Porcine: From the Ejaculation to the Fertilization Site

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Abstract

Ejaculated sperm are exposed to different environments before encountering the oocyte. However, how the sperm proteome changes during this transit remains unsolved. This study aimed to identify proteomic changes in boar sperm after incubation with male (seminal plasma, SP) and/or female (uterine fluid, UF; and oviductal fluid, OF) reproductive fluids. The following experimental groups were analyzed: (1) SP: sperm + 20% SP; (2) UF: sperm + 20% UF; (3) OF: sperm + 20% OF; (4) SP + UF: sperm + 20% SP + 20% UF; and (5) SP+OF: sperm + 20% SP + 20% OF. The proteome analysis, performed by HPLC-MS/MS, allowed the identification of 265 proteins. A total of 69 proteins were detected in the UF, SP, and SP + UF groups, and 102 proteins in the OF, SP, and SP + OF groups. Our results showed a higher number of proteins when sperm were incubated with only one fluid than when they were co-incubated with two fluids. Additionally, the number of sperm-interacting proteins from the UF group was lower than the OF group. In conclusion, the interaction of sperm with reproductive fluids alters its proteome. The description of sperm-interacting proteins in porcine species after co-incubation with male and/or female reproductive fluids may be useful to understand sperm transport, selection, capacitation, or fertilization phenomena.

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Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources.

Da Huang, Brad T. Sherman, Richard A. Lempicki (2009)

DAVID bioinformatics resources consists of an integrated biological knowledgebase and analytic tools aimed at systematically extracting biological meaning from large gene/protein lists. This protocol explains how to use DAVID, a high-throughput and integrated data-mining environment, to analyze gene lists derived from high-throughput genomic experiments. The procedure first requires uploading a gene list containing any number of common gene identifiers followed by analysis using one or more text and pathway-mining tools such as gene functional classification, functional annotation chart or clustering and functional annotation table. By following this protocol, investigators are able to gain an in-depth understanding of the biological themes in lists of genes that are enriched in genome-scale studies.

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UniProt: a worldwide hub of protein knowledge

(2018)

Abstract The UniProt Knowledgebase is a collection of sequences and annotations for over 120 million proteins across all branches of life. Detailed annotations extracted from the literature by expert curators have been collected for over half a million of these proteins. These annotations are supplemented by annotations provided by rule based automated systems, and those imported from other resources. In this article we describe significant updates that we have made over the last 2 years to the resource. We have greatly expanded the number of Reference Proteomes that we provide and in particular we have focussed on improving the number of viral Reference Proteomes. The UniProt website has been augmented with new data visualizations for the subcellular localization of proteins as well as their structure and interactions. UniProt resources are available under a CC-BY (4.0) license via the web at https://www.uniprot.org/.

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STRING v10: protein–protein interaction networks, integrated over the tree of life

Damian Szklarczyk, Andrea Franceschini, Stefan Wyder … (2014)

The many functional partnerships and interactions that occur between proteins are at the core of cellular processing and their systematic characterization helps to provide context in molecular systems biology. However, known and predicted interactions are scattered over multiple resources, and the available data exhibit notable differences in terms of quality and completeness. The STRING database (http://string-db.org) aims to provide a critical assessment and integration of protein–protein interactions, including direct (physical) as well as indirect (functional) associations. The new version 10.0 of STRING covers more than 2000 organisms, which has necessitated novel, scalable algorithms for transferring interaction information between organisms. For this purpose, we have introduced hierarchical and self-consistent orthology annotations for all interacting proteins, grouping the proteins into families at various levels of phylogenetic resolution. Further improvements in version 10.0 include a completely redesigned prediction pipeline for inferring protein–protein associations from co-expression data, an API interface for the R computing environment and improved statistical analysis for enrichment tests in user-provided networks.

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Author and article information

Journal

Journal ID (nlm-ta): Int J Mol Sci

Journal ID (iso-abbrev): Int J Mol Sci

Journal ID (publisher-id): ijms

Title: International Journal of Molecular Sciences

Publisher: MDPI

ISSN (Electronic): 1422-0067

Publication date (Electronic): 22 August 2020

Publication date Collection: September 2020

Volume: 21

Issue: 17

Electronic Location Identifier: 6060

Affiliations

[1 ]Department of Physiology, Veterinary School, International Excellence Campus for Higher Education and Research (Campus Mare Nostrum), University of Murcia, 30100 Murcia, Spain; chiara.luongo@ 123456um.es

[2 ]Department of Cell Biology and Histology, Faculty of Medicine, University of Murcia, 30100 Murcia, Spain; leopoldo.gonzalez@ 123456um.es (L.G.-B.); paula.cotsr@ 123456um.es (P.C.-R.); mjoseir@ 123456um.es (M.J.I.-R.)

[3 ]Institute for Biomedical Research of Murcia, IMIB-Arrixaca, 30100 Murcia, Spain

Author notes

[* ]Correspondence: maviles@ 123456um.es (M.A.); fagarcia@ 123456um.es (F.A.G.-V.)

[†]

These authors contributed equally to this work.

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Leopoldo González-Brusi https://orcid.org/0000-0002-6371-6423

Manuel Avilés https://orcid.org/0000-0003-4396-4718

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Publisher ID: ijms-21-06060

DOI: 10.3390/ijms21176060

PMC ID: 7570189

PubMed ID: 32842715

SO-VID: 6d4a881e-8dd6-4e3a-a54f-ff71a92b33ff

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Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

Sperm Proteome after Interaction with Reproductive Fluids in Porcine: From the Ejaculation to the Fertilization Site

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Higher order chromatin architecture

Most cited references 135

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources.

UniProt: a worldwide hub of protein knowledge

STRING v10: protein–protein interaction networks, integrated over the tree of life

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