Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.

Semenogelin I (SEMG1) is found in human semen coagulum and on the surface of spermatozoa bound to EPPIN. The physiological significance of the SEMG1/EPPIN interaction on the surface of spermatozoa is its capacity to modulate sperm progressive motility. The present study investigates the hypothesis t...

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Autores principales:	Erick J R Silva, Katherine G Hamil, Michael G O'Rand
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/375ddfd6a5db47568b1663c9aa9ee2d7
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spelling	oai:doaj.org-article:375ddfd6a5db47568b1663c9aa9ee2d72021-11-18T08:43:53ZInteracting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.1932-620310.1371/journal.pone.0082014https://doaj.org/article/375ddfd6a5db47568b1663c9aa9ee2d72013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24312623/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Semenogelin I (SEMG1) is found in human semen coagulum and on the surface of spermatozoa bound to EPPIN. The physiological significance of the SEMG1/EPPIN interaction on the surface of spermatozoa is its capacity to modulate sperm progressive motility. The present study investigates the hypothesis that the interacting surface of SEMG1 and EPPIN co-evolved within the Hominoidea time scale, as a result of adaptive pressures applied by their roles in sperm protection and reproductive fitness. Our results indicate that some amino acid residues of SEMG1 and EPPIN possess a remarkable deficiency of variation among hominoid primates. We observe a distinct residue change unique to humans within the EPPIN sequence containing a SEMG1 interacting surface, namely His92. In addition, Bayes Empirical Bayes analysis for positive selection indicates that the SEMG1 Cys239 residue underwent positive selection in humans, probably as a consequence of its role in increasing the binding affinity of these interacting proteins. We confirm the critical role of Cys239 residue for SEMG1 binding to EPPIN and inhibition of sperm motility by showing that recombinant SEMG1 mutants in which Cys239 residue was changed to glycine, aspartic acid, histidine, serine or arginine have reduced capacity to interact to EPPIN and to inhibit human sperm motility in vitro. In conclusion, our results indicate that EPPIN and SEMG1 rapidly co-evolved in primates due to their critical role in the modulation of sperm motility in the semen coagulum, providing unique insights into the molecular co-evolution of sperm surface interacting proteins.Erick J R SilvaKatherine G HamilMichael G O'RandPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 12, p e82014 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Erick J R Silva Katherine G Hamil Michael G O'Rand Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
description	Semenogelin I (SEMG1) is found in human semen coagulum and on the surface of spermatozoa bound to EPPIN. The physiological significance of the SEMG1/EPPIN interaction on the surface of spermatozoa is its capacity to modulate sperm progressive motility. The present study investigates the hypothesis that the interacting surface of SEMG1 and EPPIN co-evolved within the Hominoidea time scale, as a result of adaptive pressures applied by their roles in sperm protection and reproductive fitness. Our results indicate that some amino acid residues of SEMG1 and EPPIN possess a remarkable deficiency of variation among hominoid primates. We observe a distinct residue change unique to humans within the EPPIN sequence containing a SEMG1 interacting surface, namely His92. In addition, Bayes Empirical Bayes analysis for positive selection indicates that the SEMG1 Cys239 residue underwent positive selection in humans, probably as a consequence of its role in increasing the binding affinity of these interacting proteins. We confirm the critical role of Cys239 residue for SEMG1 binding to EPPIN and inhibition of sperm motility by showing that recombinant SEMG1 mutants in which Cys239 residue was changed to glycine, aspartic acid, histidine, serine or arginine have reduced capacity to interact to EPPIN and to inhibit human sperm motility in vitro. In conclusion, our results indicate that EPPIN and SEMG1 rapidly co-evolved in primates due to their critical role in the modulation of sperm motility in the semen coagulum, providing unique insights into the molecular co-evolution of sperm surface interacting proteins.
format	article
author	Erick J R Silva Katherine G Hamil Michael G O'Rand
author_facet	Erick J R Silva Katherine G Hamil Michael G O'Rand
author_sort	Erick J R Silva
title	Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
title_short	Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
title_full	Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
title_fullStr	Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
title_full_unstemmed	Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.
title_sort	interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin i to eppin.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/375ddfd6a5db47568b1663c9aa9ee2d7
work_keys_str_mv	AT erickjrsilva interactingproteinsonhumanspermatozoaadaptiveevolutionofthebindingofsemenogelinitoeppin AT katherineghamil interactingproteinsonhumanspermatozoaadaptiveevolutionofthebindingofsemenogelinitoeppin AT michaelgorand interactingproteinsonhumanspermatozoaadaptiveevolutionofthebindingofsemenogelinitoeppin
_version_	1718421375752863744

Interacting proteins on human spermatozoa: adaptive evolution of the binding of semenogelin I to EPPIN.

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