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

Hansson, Karin M LU ; Kjellberg, Margareta LU and Fernlund, Per LU (2009) In Toxicon 54. p.128-137
Abstract
beta-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... (More)
beta-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 degrees 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. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Toxicon
volume
54
pages
128 - 137
publisher
Elsevier
external identifiers
  • wos:000267309500006
  • pmid:19341830
  • scopus:67349280212
ISSN
0041-0101
DOI
10.1016/j.toxicon.2009.03.023
language
English
LU publication?
yes
id
65b2b576-0f13-4c36-b7e7-c17aa62025cf (old id 1392508)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/19341830?dopt=Abstract
date added to LUP
2009-05-04 15:38:56
date last changed
2017-01-01 07:29:39
@article{65b2b576-0f13-4c36-b7e7-c17aa62025cf,
  abstract     = {beta-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 degrees 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.},
  author       = {Hansson, Karin M and Kjellberg, Margareta and Fernlund, Per},
  issn         = {0041-0101},
  language     = {eng},
  pages        = {128--137},
  publisher    = {Elsevier},
  series       = {Toxicon},
  title        = {Cysteine-rich secretory proteins in snake venoms form high affinity complexes with human and porcine beta-microseminoproteins.},
  url          = {http://dx.doi.org/10.1016/j.toxicon.2009.03.023},
  volume       = {54},
  year         = {2009},
}