Roles of tyrosine-rich precursor glycoproteins and dityrosine-/DOPA-mediated protein crosslinking in oocyst wall assembly in the coccidian parasite, Eimeria maxima

Belli, S; Wallach, M; Luxford, C; Davies, MJ; Smith, NC

Roles of tyrosine-rich precursor glycoproteins and dityrosine-/DOPA-mediated protein crosslinking in oocyst wall assembly in the coccidian parasite, Eimeria maxima

Belli, S Wallach, M Luxford, C Davies, MJ Smith, NC

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Publisher:: American Society for Microbiology
Publication Type:: Journal Article
Citation:: Eukaryotic Cell, 2003, 2 (3), pp. 456 - 464
Issue Date:: 2003-01

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Field	Value	Language
dc.contributor.author	Belli, S	en_US
dc.contributor.author	Wallach, M	en_US
dc.contributor.author	Luxford, C	en_US
dc.contributor.author	Davies, MJ	en_US
dc.contributor.author	Smith, NC https://orcid.org/0000-0002-7467-1451	en_US
dc.date.issued	2003-01	en_US
dc.identifier.citation	Eukaryotic Cell, 2003, 2 (3), pp. 456 - 464	en_US
dc.identifier.issn	1535-9778	en_US
dc.identifier.uri	http://hdl.handle.net/10453/9561
dc.description.abstract	The oocyst wall of apicomplexan parasites protects them from the harsh external environment, preserving their survival prior to transmission to the next host. If oocyst wall formation could be disrupted, then logically, the cycle of disease transmission could be stopped, and strategies to control infection by several organisms of medical and veterinary importance such as Eimeria, Plasmodium, Toxoplasma, Cyclospora, and Neospora could be developed. Here, we show that two tyrosine-rich precursor glycoproteins, gam56 and gam82, found in specialized organelles (wall-forming bodies) in the sexual stage (macrogamete) of Eimeria maxima are proteolytically processed into smaller glycoproteins, which are then incorporated into the developing oocyst wall. The identification of high concentrations of dityrosine and 3,4-dihydroxyphenylalanine (DOPA) in oocyst extracts by high-pressure liquid chromatography, together with the detection of a UV autofluorescence in intact oocysts, implicates dityrosine- and possibly DOPA-protein cross-links in oocyst wall hardening. In addition, the identification of peroxidase activity in the wall-forming bodies of macrogametes supports the hypothesis that dityrosine- and DOPA-mediated cross-linking might be an enzyme-catalyzed event. As such, the mechanism of oocyst wall formation in Eimeria, is analogous to the underlying mechanisms involved in the stabilization of extracellular matrices in a number of organisms, widely distributed in nature, including insect	en_US
dc.publisher	American Society for Microbiology	en_US
dc.relation.ispartof	Eukaryotic Cell	en_US
dc.relation.isbasedon	10.1128/EC.2.3.456¿464.2003	en_US
dc.subject.classification	Microbiology	en_US
dc.title	Roles of tyrosine-rich precursor glycoproteins and dityrosine-/DOPA-mediated protein crosslinking in oocyst wall assembly in the coccidian parasite, Eimeria maxima	en_US
dc.type	Journal Article
utslib.citation.volume	3	en_US
utslib.citation.volume	2	en_US
utslib.for	110309 Infectious Diseases	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Faculty of Science/School of Life Sciences
utslib.copyright.status	closed_access
pubs.consider-herdc	false	en_US
pubs.issue	3	en_US
pubs.volume	2	en_US

Abstract:

The oocyst wall of apicomplexan parasites protects them from the harsh external environment, preserving their survival prior to transmission to the next host. If oocyst wall formation could be disrupted, then logically, the cycle of disease transmission could be stopped, and strategies to control infection by several organisms of medical and veterinary importance such as Eimeria, Plasmodium, Toxoplasma, Cyclospora, and Neospora could be developed. Here, we show that two tyrosine-rich precursor glycoproteins, gam56 and gam82, found in specialized organelles (wall-forming bodies) in the sexual stage (macrogamete) of Eimeria maxima are proteolytically processed into smaller glycoproteins, which are then incorporated into the developing oocyst wall. The identification of high concentrations of dityrosine and 3,4-dihydroxyphenylalanine (DOPA) in oocyst extracts by high-pressure liquid chromatography, together with the detection of a UV autofluorescence in intact oocysts, implicates dityrosine- and possibly DOPA-protein cross-links in oocyst wall hardening. In addition, the identification of peroxidase activity in the wall-forming bodies of macrogametes supports the hypothesis that dityrosine- and DOPA-mediated cross-linking might be an enzyme-catalyzed event. As such, the mechanism of oocyst wall formation in Eimeria, is analogous to the underlying mechanisms involved in the stabilization of extracellular matrices in a number of organisms, widely distributed in nature, including insect

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http://hdl.handle.net/10453/9561