This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Google Scholar
Google Scholar
Right arrow Articles by Abhyankar, M. M.
Right arrow Articles by Gilchrist, C. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Abhyankar, M. M.
Right arrow Articles by Gilchrist, C. A.

 Previous Article  |  Next Article 

Eukaryotic Cell, September 2008, p. 1565-1572, Vol. 7, No. 9
1535-9778/08/$08.00+0     doi:10.1128/EC.00123-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Characterization of an Entamoeba histolytica High-Mobility-Group Box Protein Induced during Intestinal Infection {triangledown} ,{dagger}

Mayuresh M. Abhyankar,1 Amelia E. Hochreiter,1,2 Jessica Hershey,2 Clive Evans,4 Yan Zhang,4 Oswald Crasta,4 Bruno W. S. Sobral,4 Barbara J. Mann,1,2 William A. Petri Jr.,1,2,3* and Carol A. Gilchrist1

Departments of Medicine,1 Microbiology,2 Pathology, University of Virginia, Charlottesville, Virginia,3 Virginia Bioinformatics Institute, Virginia Tech, Blacksburg, Virginia4

Received 8 April 2008/ Accepted 4 July 2008

The unicellular eukaryote Entamoeba histolytica is a human parasite that causes amebic dysentery and liver abscess. A genome-wide analysis of gene expression modulated by intestinal colonization and invasion identified an upregulated transcript that encoded a putative high-mobility-group box (HMGB) protein, EhHMGB1. We tested if EhHMGB1 encoded a functional HMGB protein and determined its role in control of parasite gene expression. Recombinant EhHMGB1 was able to bend DNA in vitro, a characteristic of HMGB proteins. Core conserved residues required for DNA bending activity in other HMGB proteins were demonstrated by mutational analysis to be essential for EhHMGB1 activity. EhHMGB1 was also able to enhance the binding of human p53 to its cognate DNA sequence in vitro, which is expected for an HMGB1 protein. Confocal microscopy, using antibodies against the recombinant protein, confirmed its nuclear localization. Overexpression of EhHMGB1 in HM1:IMSS trophozoites led to modulation of 33 transcripts involved in a variety of cellular functions. Of these, 20 were also modulated at either day 1 or day 29 in the mouse model of intestinal amebiasis. Notably, four transcripts with known roles in virulence, including two encoding Gal/GalNAc lectin light chains, were modulated in response to EhHMGB1 overexpression. We concluded that EhHMGB1 was a bona fide HMGB protein with the capacity to recapitulate part of the modulation of parasite gene expression seen during adaptation to the host intestine.

* Corresponding author. Mailing address: Division of Infectious Diseases and International Health, P.O. Box 801340, Charlottesville, VA 22908-1340. Phone: (434) 924-5621. Fax: (434) 924-0075. E-mail: wap3g{at}virginia.edu

{triangledown} Published ahead of print on 25 July 2008.

{dagger} Supplemental material for this article may be found at http://ec.asm.org/.

Eukaryotic Cell, September 2008, p. 1565-1572, Vol. 7, No. 9
1535-9778/08/$08.00+0     doi:10.1128/EC.00123-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»