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Structured illumination microscopy reveals actin I localization in discreet foci in Plasmodium berghei gametocytes.
Curra, Chiara; McMillan, Paul J; Spanos, Lefteris; Mollard, Vanessa; Deligianni, Elena; McFadden, Geoffrey; Tilley, Leann; Siden-Kiamos, Inga.
Affiliation
  • Curra C; Institute of Molecular Biology and Biotechnology, FORTH, Heraklion, Greece.
  • McMillan PJ; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, 3051 VIC, Australia; Biological Optical Microscopy Platform, The University of Melbourne, Melbourne, 3051 VIC, Australia.
  • Spanos L; Institute of Molecular Biology and Biotechnology, FORTH, Heraklion, Greece.
  • Mollard V; School of BioSciences, The University of Melbourne, Melbourne, 3051 VIC, Australia.
  • Deligianni E; Institute of Molecular Biology and Biotechnology, FORTH, Heraklion, Greece.
  • McFadden G; School of BioSciences, The University of Melbourne, Melbourne, 3051 VIC, Australia.
  • Tilley L; Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, 3051 VIC, Australia.
  • Siden-Kiamos I; Institute of Molecular Biology and Biotechnology, FORTH, Heraklion, Greece. Electronic address: inga@imbb.forth.gr.
Exp Parasitol ; 181: 82-87, 2017 Oct.
Article de En | MEDLINE | ID: mdl-28803903
ABSTRACT
Actin has important roles in Plasmodium parasites but its exact function in different life stages is not yet fully elucidated. Here we report the localization of ubiquitous actin I in gametocytes of the rodent model parasite P. berghei. Using an antibody specifically recognizing F-actin and deconvolution microscopy we detected actin I in a punctate pattern in gametocytes. 3D-Structured Illumination Microscopy which allows sub-diffraction limit imaging resolved the signal into structures of less than 130 nm length. A portion of actin I was soluble, but the protein was also found complexed in a stabilized form which could only be completely solubilized by treatment with SDS. An additional population of actin was pelleted at 100 000 × g, consistent with F-actin. Our results suggest that actin in this non-motile form of the parasite is present in short filaments cross-linked to other structures in a cytoskeleton.
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Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Plasmodium berghei / Actines Limites: Animals Langue: En Journal: Exp Parasitol Année: 2017 Type de document: Article Pays d'affiliation: Grèce

Texte intégral: 1 Collection: 01-internacional Base de données: MEDLINE Sujet principal: Plasmodium berghei / Actines Limites: Animals Langue: En Journal: Exp Parasitol Année: 2017 Type de document: Article Pays d'affiliation: Grèce