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dc.contributor.authorWillis, Charlene
dc.contributor.authorWang, Conan K
dc.contributor.authorOsman, Asiah
dc.contributor.authorSimon, Anne
dc.contributor.authorPickering, Darren
dc.contributor.authorMulvenna, Jason
dc.contributor.authorRiboldi-Tunicliffe, Alan
dc.contributor.authorJones, Malcolm K
dc.contributor.authorLoukas, Alex
dc.contributor.authorHofmann, Andreas
dc.date.accessioned2017-05-03T15:19:01Z
dc.date.available2017-05-03T15:19:01Z
dc.date.issued2011
dc.date.modified2012-02-13T05:07:44Z
dc.identifier.issn1932-6203
dc.identifier.doi10.1371/journal.pone.0025369
dc.identifier.urihttp://hdl.handle.net/10072/42480
dc.description.abstractSaposin-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.
dc.description.peerreviewedYes
dc.description.publicationstatusYes
dc.format.extent414421 bytes
dc.format.mimetypeapplication/pdf
dc.languageEnglish
dc.language.isoeng
dc.publisherPublic Library of Science
dc.publisher.placeUnited States
dc.relation.ispartofstudentpublicationN
dc.relation.ispartofpagefrome25369-1
dc.relation.ispartofpagetoe25369-10
dc.relation.ispartofissue10
dc.relation.ispartofjournalPloS One
dc.relation.ispartofvolume6
dc.rights.retentionY
dc.subject.fieldofresearchStructural biology (incl. macromolecular modelling)
dc.subject.fieldofresearchcode310112
dc.titleInsights into the Membrane Interactions of the Saposin-Like Proteins Na-SLP-1 and Ac-SLP-1 from Human and Dog Hookworm
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttp://www.plos.org/journals/license.html
gro.facultyGriffith Health, Griffith University Medical Research College
gro.rights.copyright© 2011, Willis et al. This is an Open Access article distributed under the terms of the Creative Commons Attribution License CCAL. (http://www.plos.org/journals/license.html)
gro.date.issued2011
gro.hasfulltextFull Text
gro.griffith.authorWillis, Charlene


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