PfSETvs methylation of histone H3K36 represses virulence genes in Plasmodium falciparum View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2013-07-03

AUTHORS

Lubin Jiang, Jianbing Mu, Qingfeng Zhang, Ting Ni, Prakash Srinivasan, Kempaiah Rayavara, Wenjing Yang, Louise Turner, Thomas Lavstsen, Thor G. Theander, Weiqun Peng, Guiying Wei, Qingqing Jing, Yoshiyuki Wakabayashi, Abhisheka Bansal, Yan Luo, José M.C. Ribeiro, Artur Scherf, L. Aravind, Jun Zhu, Keji Zhao, Louis H. Miller

ABSTRACT

The variant antigen Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1), which is expressed on the surface of P. falciparum-infected red blood cells, is a critical virulence factor for malaria. Each parasite has 60 antigenically distinct var genes that each code for a different PfEMP1 protein. During infection the clonal parasite population expresses only one gene at a time before switching to the expression of a new variant antigen as an immune-evasion mechanism to avoid the host antibody response. The mechanism by which 59 of the 60 var genes are silenced remains largely unknown. Here we show that knocking out the P. falciparum variant-silencing SET gene (here termed PfSETvs), which encodes an orthologue of Drosophila melanogaster ASH1 and controls histone H3 lysine 36 trimethylation (H3K36me3) on var genes, results in the transcription of virtually all var genes in the single parasite nuclei and their expression as proteins on the surface of individual infected red blood cells. PfSETvs-dependent H3K36me3 is present along the entire gene body, including the transcription start site, to silence var genes. With low occupancy of PfSETvs at both the transcription start site of var genes and the intronic promoter, expression of var genes coincides with transcription of their corresponding antisense long noncoding RNA. These results uncover a previously unknown role of PfSETvs-dependent H3K36me3 in silencing var genes in P. falciparum that might provide a general mechanism by which orthologues of PfSETvs repress gene expression in other eukaryotes. PfSETvs knockout parasites expressing all PfEMP1 proteins may also be applied to the development of a malaria vaccine. More... »

PAGES

223-227

Journal

TITLE

Nature

ISSUE

7457

VOLUME

499

Author Affiliations

  • Key Laboratory of Molecular Virology & Immunology, Unit of Human Parasite Molecular and Cell Biology, Institut Pasteur of Shanghai, Chinese Academy of Sciences; Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 320 Yueyang Road, Shanghai 200031, P.R. China
  • Laboratory of Malaria and Vector Research, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Rockville, Maryland 20852 USA
  • CNRS, URA 2581, F-75015 Paris, France
  • State Key Laboratory of Genetics Engineering & MOE Key Laboratory of Contemporary Anthropology, School of Life Sciences, Fudan University, Shanghai 200433, P.R. China
  • Genetics and Development Biology Center, National Heart Lung Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
  • Centre for Medical Parasitology, Department of International Health, Immunology & Microbiology, Faculty of Health Sciences, University of Copenhagen and Department of Infectious Diseases, Copenhagen University Hospital (Rigshospitalet), Copenhagen, Denmark
  • Department of Physics, George Washington University, 725 21st Street NW, Washington, D.C. 20052, USA
  • Institute of Infectious Diseases and Vaccine Development, Tongji University School of Medicine, Shanghai 200092, P.R. China
  • National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD 20894, USA
  • Systems Biology Center, National Heart Lung Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA
  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nature12361

    DOI

    http://dx.doi.org/10.1038/nature12361

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1015005829

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/23823717


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