New Insights into the Phylogeny and Gene Context Analysis of Binder of Sperm Proteins (BSPs).
Seminal plasma (SP) proteins support the survival of spermatozoa acting not only at the plasma membrane but also by inhibition of capacitation, resulting in higher fertilizing ability. Among SP proteins, BSP (binder of sperm) proteins are the most studied, since they may be useful for the improvement of semen diluents, storage and subsequent fertilization results. However, an updated and detailed phylogenetic analysis of the BSP protein superfamily has not been carried out with all the sequences described in the main databases. The update view shows for the first time an equally distributed number of sequences between the three families: BSP, and their homologs 1 (BSPH1) and 2 (BSPH2). The BSP family is divided in four subfamilies, BSP1 subfamily being the predominant, followed by subfamilies BSP3, BSP5 and BSP2. BSPH proteins were found among placental mammals (Eutheria) belonging to the orders Proboscidea, Primates, Lagomorpha, Rodentia, Chiroptera, Perissodactyla and Cetartiodactyla. However, BSPH2 proteins were also found in the Scandentia order and Metatheria clade. This phylogenetic analysis, when combined with a gene context analysis, showed a completely new evolutionary scenario for the BSP superfamily of proteins with three defined different gene patterns, one for BSPs, one for BSPH1/BSPH2/ELSPBP1 and another one for BSPH1/BSPH2 without ELSPBP1. In addition, the study has permitted to define concise conserved blocks for each family (BSP, BSPH1 and BSPH2), which could be used for a more reliable assignment for the incoming sequences, for data curation of current databases, and for cloning new BSPs, as the one described in this paper, ram seminal vesicle 20 kDa protein (RSVP20, Ovis aries BSP5b).
Departamento de Bioquímica y Biología Molecular y Celular-Instituto Universitario de Investigación en Ciencias Ambientales de Aragón (IUCA), Facultad de Veterinaria, Universidad de Zaragoza, 50013, Zaragoza, Spain.
Edith
E
Serrano
Department of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, E-30100, Murcia, Spain; Murcia Biomedical Research Institute (IMIB-Arrixaca), 30120, Murcia, Spain.
Ana B
AB
Martínez
Departamento de Bioquímica y Biología Molecular y Celular-Instituto Universitario de Investigación en Ciencias Ambientales de Aragón (IUCA), Facultad de Veterinaria, Universidad de Zaragoza, 50013, Zaragoza, Spain.
Diana
D
Arruga
Departamento de Bioquímica y Biología Molecular y Celular-Instituto Universitario de Investigación en Ciencias Ambientales de Aragón (IUCA), Facultad de Veterinaria, Universidad de Zaragoza, 50013, Zaragoza, Spain.
Rosaura
R
Pérez-Pé
Department of Biochemistry and Molecular Biology-A, Faculty of Biology, Regional Campus of International Excellence "Campus Mare Nostrum", University of Murcia, Campus Espinardo, E-30100, Murcia, Spain; Murcia Biomedical Research Institute (IMIB-Arrixaca), 30120, Murcia, Spain.
Álvaro
Á
Sánchez-Ferrer
Departamento de Bioquímica y Biología Molecular y Celular-Instituto Universitario de Investigación en Ciencias Ambientales de Aragón (IUCA), Facultad de Veterinaria, Universidad de Zaragoza, 50013, Zaragoza, Spain.
Teresa
T
Muiño-Blanco
Departamento de Bioquímica y Biología Molecular y Celular-Instituto Universitario de Investigación en Ciencias Ambientales de Aragón (IUCA), Facultad de Veterinaria, Universidad de Zaragoza, 50013, Zaragoza, Spain.
José A
JA
Cebrián-Pérez
D000595:Amino Acid Sequence; D000818:Animals; D008297:Male; D008969:Molecular Sequence Data; D010802:Phylogeny; D011485:Protein Binding; D029607:Seminal Vesicle Secretory Proteins / Q000737:chemistry / Q000145:classification* / Q000235:genetics*; D013094:Spermatozoa / Q000378:metabolism*
D029607:Seminal Vesicle Secretory Proteins