ALBERT — All Library Books, journals and Electronic Records Telegrafenberg

Hits per page

hits 1 - 4 | 4 hits

Sorting

Unknown

A newly discovered protein export machine in malaria parasites (2009)

T. F. de Koning-Ward ; P. R. Gilson ; J. A. Boddey ; [et al.]

Nature Publishing Group (NPG)

In: Nature. 459(7249): 945-9. doi: 10.1038/nature08104.

add to mindlist on the mindlist

Details

Publication Date: 2009-06-19

Description: Several hundred malaria parasite proteins are exported beyond an encasing vacuole and into the cytosol of the host erythrocyte, a process that is central to the virulence and viability of the causative Plasmodium species. The trafficking machinery responsible for this export is unknown. Here we identify in Plasmodium falciparum a translocon of exported proteins (PTEX), which is located in the vacuole membrane. The PTEX complex is ATP-powered, and comprises heat shock protein 101 (HSP101; a ClpA/B-like ATPase from the AAA+ superfamily, of a type commonly associated with protein translocons), a novel protein termed PTEX150 and a known parasite protein, exported protein 2 (EXP2). EXP2 is the potential channel, as it is the membrane-associated component of the core PTEX complex. Two other proteins, a new protein PTEX88 and thioredoxin 2 (TRX2), were also identified as PTEX components. As a common portal for numerous crucial processes, this translocon offers a new avenue for therapeutic intervention.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725363/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725363/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Koning-Ward, Tania F -- Gilson, Paul R -- Boddey, Justin A -- Rug, Melanie -- Smith, Brian J -- Papenfuss, Anthony T -- Sanders, Paul R -- Lundie, Rachel J -- Maier, Alexander G -- Cowman, Alan F -- Crabb, Brendan S -- R01 AI044008-11/AI/NIAID NIH HHS/ -- R01 AI44008/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2009 Jun 18;459(7249):945-9. doi: 10.1038/nature08104.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Walter & Eliza Hall Institute of Medical Research, Melbourne 3052, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19536257" target="_blank"〉PubMed〈/a〉

Keywords: Animals ; Animals, Genetically Modified ; Malaria, Falciparum/*parasitology ; Models, Biological ; Multiprotein Complexes/*chemistry/*metabolism ; Plasmodium falciparum/*metabolism ; Protein Binding ; Protein Transport ; Protozoan Proteins/*metabolism

Print ISSN: 0028-0836

Electronic ISSN: 1476-4687

Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics

Published by Nature Publishing Group (NPG)

Permalink

	Location	Call Number	Expected	Availability

Others were also interested in ...

PAPER CURRENT

S·F·X

Fulltext

Unknown

Targeting malaria virulence and remodeling proteins to the host erythrocyte (2004)

M. Marti ; R. T. Good ; M. Rug ; [et al.]

American Association for the Advancement of Science (AAAS)

In: Science. 306(5703): 1930-3. doi: 10.1126/science.1102452.

add to mindlist on the mindlist

Details

Publication Date: 2004-12-14

Description: To establish infection in the host, malaria parasites export remodeling and virulence proteins into the erythrocyte. These proteins can traverse a series of membranes, including the parasite membrane, the parasitophorous vacuole membrane, and the erythrocyte membrane. We show that a conserved pentameric sequence plays a central role in protein export into the host cell and predict the exported proteome in Plasmodium falciparum. We identified 400 putative erythrocyte-targeted proteins corresponding to approximately 8% of all predicted genes, with 225 virulence proteins and a further 160 proteins likely to be involved in remodeling of the host erythrocyte. The conservation of this signal across Plasmodium species has implications for the development of new antimalarials.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marti, Matthias -- Good, Robert T -- Rug, Melanie -- Knuepfer, Ellen -- Cowman, Alan F -- R01-A144008-04A1/PHS HHS/ -- New York, N.Y. -- Science. 2004 Dec 10;306(5703):1930-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Walter and Eliza Hall Institute of Medical Research, Melbourne, Victoria 3050, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15591202" target="_blank"〉PubMed〈/a〉

Keywords: *Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Computational Biology ; Cytoplasm/metabolism ; Erythrocyte Membrane/metabolism ; Gene Expression Profiling ; Genes, Protozoan ; Humans ; Hydrophobic and Hydrophilic Interactions ; Malaria, Falciparum/parasitology ; Membrane Proteins/chemistry/metabolism ; Molecular Sequence Data ; Oligonucleotide Array Sequence Analysis ; Plasmodium/chemistry/genetics/metabolism ; Plasmodium falciparum/genetics/growth & development/*metabolism/*pathogenicity ; *Protein Sorting Signals ; Protein Transport ; Protozoan Proteins/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Alignment ; Vacuoles/metabolism/parasitology ; Virulence ; Virulence Factors/chemistry/genetics/*metabolism

Print ISSN: 0036-8075

Electronic ISSN: 1095-9203

Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics