The Plasmodium falciparum Artemisinin Susceptibility-Associated AP-2 Adaptin mu Subunit is Clathrin Independent and Essential for Schizont Maturation
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F20%3A00537501" target="_blank" >RIV/60077344:_____/20:00537501 - isvavai.cz</a>
Result on the web
<a href="https://mbio.asm.org/content/11/1/e02918-19" target="_blank" >https://mbio.asm.org/content/11/1/e02918-19</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1128/mBio.02918-19" target="_blank" >10.1128/mBio.02918-19</a>
Alternative languages
Result language
angličtina
Original language name
The Plasmodium falciparum Artemisinin Susceptibility-Associated AP-2 Adaptin mu Subunit is Clathrin Independent and Essential for Schizont Maturation
Original language description
The efficacy of current antimalarial drugs is threatened by reduced susceptibility of Plasmodium falciparum to artemisinin, associated with mutations in pfkelch13. Another gene with variants known to modulate the response to artemisinin encodes the mu subunit of the AP-2 adaptin trafficking complex. To elucidate the cellular role of AP-2 mu in P. falciparum, we performed a conditional gene knockout, which severely disrupted schizont organization and maturation, leading to mislocalization of key merozoite proteins. AP-2 mu is thus essential for blood-stage replication. We generated transgenic P. falciparum parasites expressing hemagglutinin-tagged AP-2 mu and examined cellular localization by fluorescence and electron microscopy. Together with mass spectrometry analysis of coimmunoprecipitating proteins, these studies identified AP-2 mu-interacting partners, including other AP-2 subunits, the K10 kelch-domain protein, and PfEHD, an effector of endocytosis and lipid mobilization, but no evidence was found of interaction with clathrin, the expected coat protein for AP-2 vesicles. In reverse immunoprecipitation experiments with a clathrin nanobody, other heterotetrameric AP-complexes were shown to interact with clathrin, but AP-2 complex subunits were absent.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10606 - Microbiology
Result continuities
Project
—
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
mBio
ISSN
2150-7511
e-ISSN
—
Volume of the periodical
11
Issue of the periodical within the volume
1
Country of publishing house
US - UNITED STATES
Number of pages
16
Pages from-to
e02918-19
UT code for WoS article
000518763400047
EID of the result in the Scopus database
2-s2.0-85079850964