Peroxidase catalysed cross-linking of an intrinsically unstructured protein via dityrosine bonds in the oocyst wall of the apicomplexan parasite, Eimeria maxima

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dc.contributor.author Mai, Kelly en_US
dc.contributor.author Smith, Nicholas en_US
dc.contributor.author Feng, Zhi-Ping en_US
dc.contributor.author Katrib, Marilyn en_US
dc.contributor.author Slapeta, Jan en_US
dc.contributor.author Slapetova, Iveta en_US
dc.contributor.author Wallach, Michael en_US
dc.contributor.author Luxford, Catherine en_US
dc.contributor.author Davies, Michael en_US
dc.contributor.author Zhang, Xuecheng en_US
dc.contributor.author Norton, Raymond en_US
dc.contributor.author Belli, Sabina en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-10-12T03:33:30Z
dc.date.available 2012-10-12T03:33:30Z
dc.date.issued 2011 en_US
dc.identifier 2011000492 en_US
dc.identifier.citation Mai Kelly et al. 2011, 'Peroxidase catalysed cross-linking of an intrinsically unstructured protein via dityrosine bonds in the oocyst wall of the apicomplexan parasite, Eimeria maxima', Elsevier Sci Ltd, vol. 41, no. 11, pp. 1157-1164. en_US
dc.identifier.issn 0020-7519 en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18170
dc.description.abstract Apicomplexan parasites such as Eimeria maxima possess a resilient oocyst wall that protects them upon excretion in host faeces and in the outside world, allowing them to survive between hosts. The wall is formed from the contents of specialised organelles - wall-forming bodies - found in macrogametes of the parasites. The presence of dityrosine in the oocyst wall suggests that peroxidase-catalysed dityrosine cross-linking of tyrosine-rich proteins from wall-forming bodies forms a matrix that is a crucial component of oocyst walls. Bioinformatic analyses showed that one of these tyrosine-rich proteins, EmGAM56, is an intrinsically unstructured protein, dominated by random coil (52-70%), with some alpha-helix (28-43%) but a relatively low percentage of beta-sheet (1-11%); this was confirmed by nuclear magnetic resonance and circular dichroism. Furthermore, the structural integrity of EmGAM56 under extreme temperatures and pH indicated its disordered nature. The intrinsic lack of structure in EmGAM56 could facilitate its incorporation into the oocyst wall in two ways: first, intrinsically unstructured proteins are highly susceptible to proteolysis, explaining the several differently-sized oocyst wall proteins derived from EmGAM56; and, second, its flexibility could facilitate cross-linking between these tyrosine-rich derivatives. An in vitro cross-linking assay was developed using a recombinant 42 kDa truncation of EmGAM56. Peroxides, in combination with plant or fungal peroxidases, catalysed the rapid formation of dityrosine cross-linked polymers of the truncated EmGAM56, as determined by western blotting and HPLC, confirming this protein's propensity to form dityrosine bonds. en_US
dc.language en_US
dc.publisher Elsevier Sci Ltd en_US
dc.relation.isbasedon http://dx.doi.org/10.1016/j.ijpara.2011.07.001 en_US
dc.title Peroxidase catalysed cross-linking of an intrinsically unstructured protein via dityrosine bonds in the oocyst wall of the apicomplexan parasite, Eimeria maxima en_US
dc.parent International Journal For Parasitology en_US
dc.journal.volume 41 en_US
dc.journal.number 11 en_US
dc.publocation Oxford en_US
dc.identifier.startpage 1157 en_US
dc.identifier.endpage 1164 en_US
dc.cauo.name SCI.Faculty of Science en_US
dc.conference Verified OK en_US
dc.for 060500 en_US
dc.personcode 02085886 en_US
dc.personcode 0000074301 en_US
dc.personcode 0000074302 en_US
dc.personcode 044726 en_US
dc.personcode 996946 en_US
dc.personcode 997043 en_US
dc.personcode 021128 en_US
dc.personcode 0000020321 en_US
dc.personcode 0000045917 en_US
dc.personcode 0000074303 en_US
dc.personcode 0000020341 en_US
dc.personcode 990003 en_US
dc.percentage 100 en_US
dc.classification.name Microbiology en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords Storage Polysaccharide; Structure Prediction; Coccidian Parasite; Disordered Regions; Alpha-Synuclein; Conformation; Antigens; Server en_US
dc.staffid 990003 en_US


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