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

DSpace/Manakin Repository

Search OPUS


Advanced Search

Browse

My Account

Show simple item record

dc.contributor.author Mai, K
dc.contributor.author Smith, NC
dc.contributor.author Feng, ZP
dc.contributor.author Katrib, M
dc.contributor.author Slapeta, J
dc.contributor.author Slapetova, I
dc.contributor.author Wallach, MG
dc.contributor.author Luxford, C
dc.contributor.author Davies, MJ
dc.contributor.author Zhang, X
dc.contributor.author Norton, RS
dc.contributor.author Belli, SI
dc.date.accessioned 2012-10-12T03:33:30Z
dc.date.issued 2011-09
dc.identifier.citation International journal for parasitology, 2011, 41 (11), pp. 1157 - 1164
dc.identifier.issn 0020-7519
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 α-helix (28-43%) but a relatively low percentage of β-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 42kDa 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.
dc.format Print-Electronic
dc.language eng
dc.relation.isbasedon 10.1016/j.ijpara.2011.07.001
dc.title Peroxidase catalysed cross-linking of an intrinsically unstructured protein via dityrosine bonds in the oocyst wall of the apicomplexan parasite, Eimeria maxima.
dc.type Journal Article
dc.parent International journal for parasitology
dc.journal.volume 11
dc.journal.volume 41
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 0605 Microbiology
dc.personcode 021128
dc.personcode 990003
dc.personcode 997043
dc.personcode 996946
dc.personcode 044726
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 Eimeria
dc.description.keywords Oocysts
dc.description.keywords Cell Wall
dc.description.keywords Tyrosine
dc.description.keywords Peroxidase
dc.description.keywords Protozoan Proteins
dc.description.keywords Cross-Linking Reagents
dc.description.keywords Protein Structure, Tertiary
dc.description.keywords Biocatalysis
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - i3
utslib.copyright.status Closed Access
utslib.copyright.date 2015-04-15 12:17:09.805752+10
pubs.consider-herdc true
utslib.collection.history Closed (ID: 3)
utslib.collection.history School of Medical and Molecular Sciences (ID: 341)


Files in this item

This item appears in the following Collection(s)

Show simple item record