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Arginine deiminase has multiple regulatory roles in the biology of Giardia lamblia
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2008 (English)In: Journal of Cell Science, ISSN 0021-9533, Vol. 121, no 17, 2930-2938 p.Article in journal (Refereed) Published
Abstract [en]

The protozoan parasite Giardia lamblia uses arginine deiminase (ADI) to produce energy from free L-arginine under anaerobic conditions. In this work, we demonstrate that, in addition to its known role as a metabolic enzyme, it also functions as a peptidylarginine deiminase, converting protein-bound arginine into citrulline. G. lamblia ADI specifically binds to and citrullinates the arginine in the conserved CRGKA tail of variant-specific surface proteins (VSPs), affecting both antigenic switching and antibody-mediated cell death. During encystation, ADI translocates from the cytoplasm to the nuclei and appears to play a regulatory role in the expression of encystation-specific genes. ADI is also sumoylated, which might modulate its activity. Our findings reveal a dual role played by ADI and define novel regulatory pathways used by Giardia for survival.

Place, publisher, year, edition, pages
2008. Vol. 121, no 17, 2930-2938 p.
Keyword [en]
arginine deiminase, citrullination, sumoylation, antigenic variation, encystation, gene regulation
National Category
Biological Sciences
URN: urn:nbn:se:uu:diva-109125DOI: 10.1242/jcs.026963ISI: 000258596600016OAI: oai:DiVA.org:uu-109125DiVA: diva2:248927
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2009-10-09Bibliographically approved

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