Cysteine-rich secretory proteins in snake venoms form high affinity complexes with human and porcine β-microseminoproteins

• Published in: Toxicon (Oxford) Vol. 54; no. 2; pp. 128 - 137
• Main Authors: Hansson, Karin, Kjellberg, Margareta, Fernlund, Per
• Format: Journal Article
• Language: English
• Published: Kidlington Elsevier Ltd 01.08.2009; Elsevier
• Subjects: Amino Acid Sequence; Animal poisons toxicology. Antivenoms; Animals; Basic Medicine; Biological and medical sciences; Chromatography, Gel; Cysteine - chemistry; Cysteine-rich secretory protein; Elapid Venoms - chemistry; Electrophoresis, Polyacrylamide Gel; Gynecology. Andrology. Obstetrics; Humans; Kinetics; Läkemedelskemi; Male genital diseases; Mass Spectrometry; Medical and Health Sciences; Medical sciences; Medicin och hälsovetenskap; Medicinal Chemistry; Medicinska och farmaceutiska grundvetenskaper; Molecular Sequence Data; Nephrology. Urinary tract diseases; Prostate cancer; Protein complex; PSP94; Semen - chemistry; Seminal plasma; Snake venom; Snake Venoms - chemistry; Surface Plasmon Resonance; Swine; Toxicology; Tumors; Tumors of the urinary system; Urinary tract. Prostate gland; Viper Venoms - chemistry; β-Microseminoprotein; Protein complex; CRISP; Snake venom; RU; PSP94; MS; Cysteine-rich secretory protein; β-Microseminoprotein; MSP; pMSP; SDS-PAGE; SGP28; hMSP; nanoESI; PSPBP; Seminal plasma; Prostate cancer; Cysteine; Prostate disease; Blood plasma; Secretory protein; Male genital diseases; Human; Urinary system disease; Semen; Animal origin; Malignant tumor; Ophidia; Vertebrata; Aminoacid; Animal; Venom; Affinity; Reptilia; Cancer
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2009.03.023

β-Microseminoprotein (MSP), a 10 kDa protein in human seminal plasma, binds human cysteine-rich secretory protein-3 (CRISP-3) with high affinity. CRISP-3 is a member of the family of CRISPs, which are widespread among animals. In this work we show that human as well as porcine MSP binds catrin, latisemin, pseudecin, and triflin, which are CRISPs present in the venoms of the snakes Crotalus atrox, Laticauda semifasciata, Pseudechis porphyriacus, and Trimeresurus flavoviridis, respectively. The CRISPs were purified from the venoms by affinity chromatography on a human MSP column and their identities were settled by gel electrophoresis and mass spectrometry. Their interactions with human and porcine MSPs were studied with size exclusion chromatography and surface plasmon resonance measurements. The binding affinities at 25 °C were between 10 −10 M and 10 −7 M for most of the interactions, with higher affinities for the interactions with porcine MSP compared to human MSP and with Elapidae CRISPs compared to Viperidae CRISPs. The high affinities of the bindings in spite of the differences in amino acid sequence between the MSPs as well as between the CRISPs indicate that the binding is tolerant to amino acid sequence variation and raise the question how universal this cross-species reaction between MSPs and CRISPs is.