Unusual properties of Plasmodium falciparum actin : new insights into microfilament dynamics of apicomplexan parasites
Schüler, Herwig LU
; Mueller, Ann-Kristin
and Matuschewski, Kai
(2005)
In FEBS Letters
579(3).
p.60-655
- Abstract
Plasmodium falciparum, the etiologic agent of malaria, is a facultative intracellular parasite of the phylum Apicomplexa. A limited turnover of microfilaments takes place beneath the parasite plasma membrane, but the cytoplasm of apicomplexans is virtually devoid of F-actin. We produced Plasmodium actin in yeast. Purified recombinant Plasmodium actin polymerized inefficiently unless both gelsolin and phalloidin were added. The resulting actin polymers appeared fragmented in the fluorescence microscope. Plasmodium actin bound DNaseI about 200 times weaker than bovine non-muscle actin. Our findings suggest that the unique properties of Plasmodium actin can explain some of the unusual features of apicomplexan parasite microfilaments.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/31f93e33-d72c-42f9-91d0-fbf5f2931682
- author
- Schüler, Herwig
LU
; Mueller, Ann-Kristin
and Matuschewski, Kai
- publishing date
- 2005-01-31
- type
- Contribution to journal
- publication status
- published
- keywords
- Actins/chemistry, Amino Acid Sequence, Animals, Cloning, Molecular, DNA, Complementary, Models, Molecular, Molecular Sequence Data, Plasmodium falciparum/metabolism, Protein Conformation, Sequence Homology, Amino Acid
- in
- FEBS Letters
- volume
- 579
- issue
- 3
- pages
- 6 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- pmid:15670824
- scopus:12744272468
- ISSN
- 0014-5793
- DOI
- 10.1016/j.febslet.2004.12.037
- language
- English
- LU publication?
- no
- id
- 31f93e33-d72c-42f9-91d0-fbf5f2931682
- date added to LUP
- 2024-11-21 18:06:54
- date last changed
- 2025-06-20 21:21:56
@article{31f93e33-d72c-42f9-91d0-fbf5f2931682,
abstract = {{<p>Plasmodium falciparum, the etiologic agent of malaria, is a facultative intracellular parasite of the phylum Apicomplexa. A limited turnover of microfilaments takes place beneath the parasite plasma membrane, but the cytoplasm of apicomplexans is virtually devoid of F-actin. We produced Plasmodium actin in yeast. Purified recombinant Plasmodium actin polymerized inefficiently unless both gelsolin and phalloidin were added. The resulting actin polymers appeared fragmented in the fluorescence microscope. Plasmodium actin bound DNaseI about 200 times weaker than bovine non-muscle actin. Our findings suggest that the unique properties of Plasmodium actin can explain some of the unusual features of apicomplexan parasite microfilaments.</p>}},
author = {{Schüler, Herwig and Mueller, Ann-Kristin and Matuschewski, Kai}},
issn = {{0014-5793}},
keywords = {{Actins/chemistry; Amino Acid Sequence; Animals; Cloning, Molecular; DNA, Complementary; Models, Molecular; Molecular Sequence Data; Plasmodium falciparum/metabolism; Protein Conformation; Sequence Homology, Amino Acid}},
language = {{eng}},
month = {{01}},
number = {{3}},
pages = {{60--655}},
publisher = {{Wiley-Blackwell}},
series = {{FEBS Letters}},
title = {{Unusual properties of <i>Plasmodium </i>falciparum actin : new insights into microfilament dynamics of apicomplexan parasites}},
url = {{http://dx.doi.org/10.1016/j.febslet.2004.12.037}},
doi = {{10.1016/j.febslet.2004.12.037}},
volume = {{579}},
year = {{2005}},
}