Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm

Willis, Charlene, Wang, Conan K., Osman, Asiah, Simon, Anne, Pickering, Darren, Mulvenna, Jason, Riboldi-Tunicliffe, Alan, Jones, Malcolm K., Loukas, Alex and Hofmann, Andreas (2011) Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm. PLoS One, 6 10: e25369.1-e25369.10. doi:10.1371/journal.pone.0025369


Author Willis, Charlene
Wang, Conan K.
Osman, Asiah
Simon, Anne
Pickering, Darren
Mulvenna, Jason
Riboldi-Tunicliffe, Alan
Jones, Malcolm K.
Loukas, Alex
Hofmann, Andreas
Title Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm
Formatted title
Insights into the membrane interactions of the saposin-like proteins Na-SLP-1 and Ac-SLP-1 from human and dog hookworm
Journal name PLoS One   Check publisher's open access policy
ISSN 1932-6203
Publication date 2011-10
Sub-type Article (original research)
DOI 10.1371/journal.pone.0025369
Open Access Status DOI
Volume 6
Issue 10
Start page e25369.1
End page e25369.10
Total pages 10
Place of publication San Francisco, CA, United States
Publisher Public Library of Science
Collection year 2012
Language eng
Abstract Saposin-like proteins (SAPLIPs) from soil-transmitted helminths play pivotal roles in host-pathogen interactions and have a high potential as targets for vaccination against parasitic diseases. We have identified two non-orthologous SAPLIPs from human and dog hookworm, Na-SLP-1 and Ac-SLP-1, and solved their three-dimensional crystal structures. Both proteins share the property of membrane binding as monitored by liposome co-pelleting assays and monolayer adsorption. Neither SAPLIP displayed any significant haemolytic or bactericidal activity. Based on the structural information, as well as the results from monolayer adsorption, we propose models of membrane interactions for both SAPLIPs. Initial membrane contact of the monomeric Na-SLP-1 is most likely by electrostatic interactions between the membrane surface and a prominent basic surface patch. In case of the dimeric Ac-SLP-1, membrane interactions are most likely initiated by a unique tryptophan residue that has previously been implicated in membrane interactions in other SAPLIPs.
Keyword Nk-lysin
Ancylostoma caninum
Crystal structure
Lipid binding
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article number e25369

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
School of Veterinary Science Publications
 
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