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

b-Microseminoprotein (MSP), a 10kDa 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, latis...

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Bibliographic Details
Published in:Toxicon (Oxford) 2009-08, Vol.54 (2), p.128-137
Main Authors: Hansson, K, Kjellberg, M, Fernlund, P
Format: Article
Language:English
Subjects:
Crotalus atrox
Elapidae
Laticauda semifasciata
Pseudechis porphyriacus
Trimeresurus flavoviridis
Viperidae
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Summary:b-Microseminoprotein (MSP), a 10kDa 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@uoC were between 10@u-@u1@u0M and 10@u-@u7M 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. electrophoresis
ISSN:0041-0101
DOI:10.1016/j.toxicon.2009.03.023