IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Gounaris, K.
Right arrow Articles by Selkirk, M. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gounaris, K.
Right arrow Articles by Selkirk, M. E.

 Previous Article  |  Next Article 

Infection and Immunity, June 2001, p. 3658-3662, Vol. 69, No. 6
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.6.3658-3662.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Secreted Variant of Nucleoside Diphosphate Kinase from the Intracellular Parasitic Nematode Trichinella spiralis

Kleoniki Gounaris,* Simon Thomas, Pilar Najarro, and Murray E. Selkirk

Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom

Received 22 December 2000/Returned for modification 11 February 2001/Accepted 7 March 2001

The molecular components involved in the survival of the parasitic nematode Trichinella spiralis in an intracellular environment are poorly characterized. Here we demonstrate that infective larvae secrete a nucleoside diphosphate kinase when maintained in vitro. The secreted enzyme forms a phosphohistidine intermediate and shows broad specificity in that it readily accepts gamma -phosphate from both ATP and GTP and donates it to all nucleoside and deoxynucleoside diphosphate acceptors tested. The enzyme was partially purified from culture medium by ATP affinity chromatography and identified as a 17-kDa protein by autophosphorylation and reactivity with an antibody to a plant-derived homologue. Secreted nucleoside diphosphate kinases have previously been identified only in prokaryotic organisms, all of them bacterial pathogens. The identification of a secreted variant of this enzyme from a multicellular eukaryote is very unusual and is suggestive of a role in modulating host cell function.

* Corresponding author. Mailing address: Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, United Kingdom. Phone: 44 20 7594 5209. Fax: 44 20 7594 5207. E-mail: k.gounaris{at}ic.ac.uk.

Infection and Immunity, June 2001, p. 3658-3662, Vol. 69, No. 6
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.6.3658-3662.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2001 by the American Society for Microbiology. All rights reserved.