FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2591933062> ?p ?o ?g. }

• W2591933062 abstract "Abstract Export of parasite proteins into the host erythrocyte is essential for survival of Plasmodium falciparum during its asexual lifecycle. While several studies described key factors within the parasite that are involved in protein export, the mechanisms employed to traffic exported proteins within the host cell are currently unknown. Members of the Hsp70 family of chaperones, together with their Hsp40 co-chaperones, facilitate protein trafficking in other organisms, and are thus likely used by P. falciparum in the trafficking of its exported proteins. A large group of Hsp40 proteins is encoded by the parasite and exported to the host cell, but only one Hsp70, PfHsp70x, is exported with them. PfHsp70x is absent from most Plasmodium species and is found only in P. falciparum and closely-related species that infect Apes. Herein, we have utilized CRISPR/Cas9 genome editing in P. falciparum to investigate the essentiality of PfHsp70x. We show that parasitic growth was unaffected by knockdown of PfHsp70x using both the DHFR-based Destabilization Domain and the glmS ribozyme system. Similarly, a complete gene knockout of PfHsp70x did not affect the ability of P. falciparum to proceed through its intraerythrocytic lifecycle. The effect of PfHsp70x knockdown/knockout on the export of proteins to the host RBC, including the critical virulence factor PfEMP1, was tested and we found that this process was unaffected. These data show that although PfHsp70x is the sole exported Hsp70, it is not essential for the asexual development of P. falciparum . Importance Half of the world’s population lives at risk for malaria. The intraerythrocytic lifecycle of Plasmodium spp. is responsible for clinical manifestations of malaria; therefore, knowledge of the parasite’s ability to survive within the erythrocyte is needed to combat the deadliest agent of malaria, P. falciparum . An outstanding question in the field is how P. falciparum undertakes the essential process of trafficking its proteins within the host cell. In most organisms, chaperones such as Hsp70 are employed in protein trafficking. Of the human-disease causing Plasmodium species, the chaperone PfHsp70x is unique to P. falciparum, and it is the only parasite protein of its kind exported to the host (1). This has placed PfHsp70x as an ideal target to inhibit protein trafficking and kill the parasite. However, we show that PfHsp70x is not required for export of parasite effectors nor is it essential for parasite survival inside of the RBC." @default.
• W2591933062 created "2017-03-16" @default.
• W2591933062 creator A5029513421 @default.
• W2591933062 creator A5031801456 @default.
• W2591933062 creator A5078009221 @default.
• W2591933062 creator A5088385803 @default.
• W2591933062 date "2017-03-03" @default.
• W2591933062 modified "2023-09-25" @default.
• W2591933062 title "The exported chaperone PfHsp70x is dispensable for the Plasmodium falciparum intraerythrocytic lifecycle" @default.
• W2591933062 cites W1526053806 @default.
• W2591933062 cites W1527127553 @default.
• W2591933062 cites W1830111561 @default.
• W2591933062 cites W1930569326 @default.
• W2591933062 cites W1940545045 @default.
• W2591933062 cites W1965043952 @default.
• W2591933062 cites W1967448179 @default.
• W2591933062 cites W1972959613 @default.
• W2591933062 cites W1973541716 @default.
• W2591933062 cites W1994076428 @default.
• W2591933062 cites W2001670495 @default.
• W2591933062 cites W2015141554 @default.
• W2591933062 cites W2024663642 @default.
• W2591933062 cites W2027266940 @default.
• W2591933062 cites W2028217000 @default.
• W2591933062 cites W2033929194 @default.
• W2591933062 cites W2034037368 @default.
• W2591933062 cites W2035205417 @default.
• W2591933062 cites W2038774660 @default.
• W2591933062 cites W2041941982 @default.
• W2591933062 cites W2049237667 @default.
• W2591933062 cites W2055730063 @default.
• W2591933062 cites W2058302605 @default.
• W2591933062 cites W2062619148 @default.
• W2591933062 cites W2068603872 @default.
• W2591933062 cites W2068928962 @default.
• W2591933062 cites W2075117194 @default.
• W2591933062 cites W2081711923 @default.
• W2591933062 cites W2097432311 @default.
• W2591933062 cites W2109735813 @default.
• W2591933062 cites W2112798524 @default.
• W2591933062 cites W2134148555 @default.
• W2591933062 cites W2156160408 @default.
• W2591933062 cites W2158718118 @default.
• W2591933062 cites W2231638149 @default.
• W2591933062 cites W2264948396 @default.
• W2591933062 cites W2322062798 @default.
• W2591933062 cites W2327503274 @default.
• W2591933062 cites W2538382920 @default.
• W2591933062 cites W2551303899 @default.
• W2591933062 cites W2726949767 @default.
• W2591933062 cites W2736767386 @default.
• W2591933062 cites W4321429278 @default.
• W2591933062 cites W920975095 @default.
• W2591933062 doi "https://doi.org/10.1101/113365" @default.
• W2591933062 hasPublicationYear "2017" @default.
• W2591933062 type Work @default.
• W2591933062 sameAs 2591933062 @default.
• W2591933062 citedByCount "0" @default.
• W2591933062 crossrefType "posted-content" @default.
• W2591933062 hasAuthorship W2591933062A5029513421 @default.
• W2591933062 hasAuthorship W2591933062A5031801456 @default.
• W2591933062 hasAuthorship W2591933062A5078009221 @default.
• W2591933062 hasAuthorship W2591933062A5088385803 @default.
• W2591933062 hasBestOaLocation W25919330621 @default.
• W2591933062 hasConcept C104317684 @default.
• W2591933062 hasConcept C144024400 @default.
• W2591933062 hasConcept C149923435 @default.
• W2591933062 hasConcept C173396325 @default.
• W2591933062 hasConcept C203014093 @default.
• W2591933062 hasConcept C2778048844 @default.
• W2591933062 hasConcept C2778371730 @default.
• W2591933062 hasConcept C2908647359 @default.
• W2591933062 hasConcept C54355233 @default.
• W2591933062 hasConcept C86803240 @default.
• W2591933062 hasConcept C95444343 @default.
• W2591933062 hasConceptScore W2591933062C104317684 @default.
• W2591933062 hasConceptScore W2591933062C144024400 @default.
• W2591933062 hasConceptScore W2591933062C149923435 @default.
• W2591933062 hasConceptScore W2591933062C173396325 @default.
• W2591933062 hasConceptScore W2591933062C203014093 @default.
• W2591933062 hasConceptScore W2591933062C2778048844 @default.
• W2591933062 hasConceptScore W2591933062C2778371730 @default.
• W2591933062 hasConceptScore W2591933062C2908647359 @default.
• W2591933062 hasConceptScore W2591933062C54355233 @default.
• W2591933062 hasConceptScore W2591933062C86803240 @default.
• W2591933062 hasConceptScore W2591933062C95444343 @default.
• W2591933062 hasLocation W25919330621 @default.
• W2591933062 hasLocation W25919330622 @default.
• W2591933062 hasOpenAccess W2591933062 @default.
• W2591933062 hasPrimaryLocation W25919330621 @default.
• W2591933062 hasRelatedWork W1828691184 @default.
• W2591933062 hasRelatedWork W1991523530 @default.
• W2591933062 hasRelatedWork W2002128513 @default.
• W2591933062 hasRelatedWork W2041559206 @default.
• W2591933062 hasRelatedWork W2065019097 @default.
• W2591933062 hasRelatedWork W2088063203 @default.
• W2591933062 hasRelatedWork W2126061209 @default.
• W2591933062 hasRelatedWork W2171277769 @default.
• W2591933062 hasRelatedWork W2560815075 @default.
• W2591933062 hasRelatedWork W2092874662 @default.

• next