The secreted and surface proteomes of the adult stage of the carcinogenic human liver fluke Opisthorchis viverrini

Mulvenna, Jason, Sripa, Bancho, Brindley, Paul J., Gorman, Jeffrey, Jones, Malcolm K., Colgrave, Michelle L., Jones, Alun, Nawaratna, Sujeevi, Laha, Thewarach, Suttiprapa, Sutas, Smout, Michael J. and Loukas, Alex (2010) The secreted and surface proteomes of the adult stage of the carcinogenic human liver fluke Opisthorchis viverrini. Proteomics, 10 5: 1063-1078. doi:10.1002/pmic.200900393

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Author Mulvenna, Jason
Sripa, Bancho
Brindley, Paul J.
Gorman, Jeffrey
Jones, Malcolm K.
Colgrave, Michelle L.
Jones, Alun
Nawaratna, Sujeevi
Laha, Thewarach
Suttiprapa, Sutas
Smout, Michael J.
Loukas, Alex
Title The secreted and surface proteomes of the adult stage of the carcinogenic human liver fluke Opisthorchis viverrini
Journal name Proteomics   Check publisher's open access policy
ISSN 1615-9853
Publication date 2010-03-05
Sub-type Article (original research)
DOI 10.1002/pmic.200900393
Volume 10
Issue 5
Start page 1063
End page 1078
Total pages 16
Place of publication Weinheim, Germany
Publisher Wiley-VCH
Collection year 2011
Language eng
Formatted abstract
Infection with the human liver fluke, Opisthorchis viverrini, is a serious public health problem in Thailand, Laos and nearby locations in Southeast Asia. Both experimental and epidemiological evidence strongly implicate liver fluke infection in the etiology of one of the liver cancer subtypes, cholangiocarcinoma (CCA). To identify parasite proteins critical for liver fluke survival and the etiology of CCA, OFFGEL electrophoresis and multiple reaction monitoring were employed to characterize 300 parasite proteins from the O. viverrini excretory/secretory products and, utilizing selective labeling and sequential solubilization, from the host-exposed tegument. The excretory/ secretory included a complex mixture of proteins that have been associated with cancers, including proteases of different mechanistic classes and orthologues of mammalian growth factors and anti-apoptotic proteins. Also identified was a cysteine protease inhibitor which, in other helminth pathogens, induces nitric oxide production by macrophages, and, hence may contribute to malignant transformation of inflamed cells. More than 160 tegumental proteins were identified using sequential solubilization of isolated teguments, and a subset of these was localized to the surface membrane of the tegument by labeling living flukes with biotin and confirming surface localization with fluorescence microscopy. These included annexins, which are potential immuno-modulators, and orthologues of the schistosomiasis vaccine antigens Sm29 and tetraspanin-2. Novel roles in pathogenesis were suggested for the tegument-host interface since more than ten surface proteins had no homologues in the public databases. The O. viverrini proteins identified here provide an extensive catalogue of novel leads for research on the pathogenesis of opisthorchiasis and the development of novel interventions for this disease and CCA, as well as providing a scaffold for sequencing the genome of this fluke.
© 2010 WILEY-VCH Verlag GmbH & Co. KGaA.
Keyword Animal proteomics
Opisthorchis viverrini
Glyceraldehyde-3-phosphate Dehydrogenase
Thioredoxin reductase
Epithelin precursor
Parasite infection
Northeast Thailand
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
School of Medicine Publications
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Citation counts: TR Web of Science Citation Count  Cited 57 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 65 times in Scopus Article | Citations
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Created: Sun, 11 Apr 2010, 00:01:05 EST