Bovine seminal plasma osteopontin: Structural modelling, recombinant expression and its relationship with semen quality
| Autor: | Jomar Pereira Laurino, Gabrielle Dias Salton, Silvio Renato Oliveira Menegassi, Rodrigo Costa Mattos, Júlio Otávio Jardim Barcellos, Marlon R. Schneider, Fernanda Mosena Munari, Gabriel Pereira, Maria Inês Mascarenhas Jobim, Elizabeth Obino Cirne-Lima, Ivan Cunha Bustamante-Filho |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Male
Urology Integrin 030232 urology & nephrology law.invention Glycosaminoglycan 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Endocrinology stomatognathic system law Semen Hyaluronic acid Animals Osteopontin Fertilisation 030219 obstetrics & reproductive medicine biology General Medicine Molecular Docking Simulation Semen Analysis Fertility chemistry Biochemistry Docking (molecular) Phosphoprotein Recombinant DNA biology.protein Cattle |
| Zdroj: | AndrologiaREFERENCES. 53(1) |
| ISSN: | 1439-0272 |
| Popis: | Osteopontin (OPN) is a multifunctional phosphoprotein that has been linked to fertility in bulls. However, the exact mechanism by which OPN contributes to fertilisation is yet unknown. The biotechnological use of OPN in bovine reproduction is promising but some gaps remain unfilled. The present work aimed: (a) to verify whether the seminal plasma OPN is associated with seminal traits and a standard breeding soundness exam; (b) to predict OPN interactions with integrins, CD44 and glycosaminoglycans through molecular docking; and (c) to develop a protocol for recombinant expression of OPN from vesicular gland cDNA. Ejaculates from top ranked bulls had higher amounts of seminal plasma OPN in comparison with bulls classified as questionable (p < .01). The structural modelling and molecular docking predictions indicated that bovine OPN binds to heparin disaccharide, hyaluronic acid and hyaluronan. In addition, docking studies described the binding complexes of OPN with CD44 and the integrin heterodimers α5β1 and αVβ3. Finally, expression of rOPN-6His was successfully obtained after 3 hr of induction with 0.5 mM IPTG at 37°C and a denaturing purification protocol resulted in efficiently purified recombinant OPN. The present results contribute to the development of biotechnological uses of OPN as a biomarker in bovine reproduction. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|