Susceptibilities of Ugandan Plasmodium falciparum Isolates to Proteasome Inhibitors
The proteasome is a promising target for antimalarial chemotherapy. We assessed susceptibilities of fresh Plasmodium falciparum isolates from eastern Uganda to seven proteasome inhibitors: two asparagine ethylenediamines, two macrocyclic peptides, and three peptide boronates; five had median IC valu...
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| Veröffentlicht in: | Antimicrobial agents and chemotherapy 2022-10, Vol.66 (10), p.e0081722-e0081722 |
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| creator | Garg, Shreeya Kreutzfeld, Oriana Chelebieva, Sevil Tumwebaze, Patrick K Byaruhanga, Oswald Okitwi, Martin Orena, Stephen Katairo, Thomas Nsobya, Samuel L Conrad, Melissa D Aydemir, Ozkan Legac, Jennifer Gould, Alexandra E Bayles, Brett R Bailey, Jeffrey A Duffey, Maelle Lin, Gang Kirkman, Laura A Cooper, Roland A Rosenthal, Philip J |
| description | The proteasome is a promising target for antimalarial chemotherapy. We assessed
susceptibilities of fresh Plasmodium falciparum isolates from eastern Uganda to seven proteasome inhibitors: two asparagine ethylenediamines, two macrocyclic peptides, and three peptide boronates; five had median IC
values |
| doi_str_mv | 10.1128/aac.00817-22 |
| format | Article |
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susceptibilities of fresh Plasmodium falciparum isolates from eastern Uganda to seven proteasome inhibitors: two asparagine ethylenediamines, two macrocyclic peptides, and three peptide boronates; five had median IC
values <100 nM. TDI8304, a macrocylic peptide lead compound with drug-like properties, had a median IC
of 16 nM. Sequencing genes encoding the β2 and β5 catalytic proteasome subunits, the predicted targets of the inhibitors, and five additional proteasome subunits, identified two mutations in β2 (I204T, S214F), three mutations in β5 (V2I, A142S, D150E), and three mutations in other subunits. The β2 S214F mutation was associated with decreased susceptibility to two peptide boronates, with IC
s of 181 nM and 2635 nM against mutant versus 62 nM and 477 nM against wild type parasites for MMV1579506 and MMV1794229, respectively, although significance could not be formally assessed due to the small number of mutant parasites with available data. The other β2 and β5 mutations and mutations in other subunits were not associated with susceptibility to tested compounds. Against culture-adapted Ugandan isolates, two asparagine ethylenediamines and the peptide proteasome inhibitors WLW-vinyl sulfone and WLL-vinyl sulfone (which were not studied
) demonstrated low nM activity, without decreased activity against β2 S214F mutant parasites. Overall, proteasome inhibitors had potent activity against P. falciparum isolates circulating in Uganda, and genetic variation in proteasome targets was uncommon.</description><identifier>ISSN: 0066-4804</identifier><identifier>EISSN: 1098-6596</identifier><identifier>DOI: 10.1128/aac.00817-22</identifier><identifier>PMID: 36094216</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Antimalarials - chemistry ; Antimalarials - pharmacology ; Antimicrobial Chemotherapy ; Asparagine ; Drug Resistance - genetics ; Ethylenediamines - pharmacology ; Humans ; Malaria, Falciparum - drug therapy ; Malaria, Falciparum - parasitology ; Mechanisms of Resistance ; Peptides - pharmacology ; Plasmodium falciparum - drug effects ; Plasmodium falciparum - genetics ; Proteasome Endopeptidase Complex - genetics ; Proteasome Inhibitors - chemistry ; Proteasome Inhibitors - pharmacology ; Uganda</subject><ispartof>Antimicrobial agents and chemotherapy, 2022-10, Vol.66 (10), p.e0081722-e0081722</ispartof><rights>Copyright © 2022 American Society for Microbiology.</rights><rights>Copyright © 2022 American Society for Microbiology. 2022 American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a418t-8e6fee6be3d931d01f8c0632ecc8c187d5e6aa2cd032e95afd00d2e5e0173c0b3</citedby><cites>FETCH-LOGICAL-a418t-8e6fee6be3d931d01f8c0632ecc8c187d5e6aa2cd032e95afd00d2e5e0173c0b3</cites><orcidid>0000-0003-4085-5540 ; 0000-0002-7953-7622 ; 0000-0002-9984-8030 ; 0000-0003-2026-345X ; 0000-0002-8437-9382</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9578402/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC9578402/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/36094216$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Garg, Shreeya</creatorcontrib><creatorcontrib>Kreutzfeld, Oriana</creatorcontrib><creatorcontrib>Chelebieva, Sevil</creatorcontrib><creatorcontrib>Tumwebaze, Patrick K</creatorcontrib><creatorcontrib>Byaruhanga, Oswald</creatorcontrib><creatorcontrib>Okitwi, Martin</creatorcontrib><creatorcontrib>Orena, Stephen</creatorcontrib><creatorcontrib>Katairo, Thomas</creatorcontrib><creatorcontrib>Nsobya, Samuel L</creatorcontrib><creatorcontrib>Conrad, Melissa D</creatorcontrib><creatorcontrib>Aydemir, Ozkan</creatorcontrib><creatorcontrib>Legac, Jennifer</creatorcontrib><creatorcontrib>Gould, Alexandra E</creatorcontrib><creatorcontrib>Bayles, Brett R</creatorcontrib><creatorcontrib>Bailey, Jeffrey A</creatorcontrib><creatorcontrib>Duffey, Maelle</creatorcontrib><creatorcontrib>Lin, Gang</creatorcontrib><creatorcontrib>Kirkman, Laura A</creatorcontrib><creatorcontrib>Cooper, Roland A</creatorcontrib><creatorcontrib>Rosenthal, Philip J</creatorcontrib><title>Susceptibilities of Ugandan Plasmodium falciparum Isolates to Proteasome Inhibitors</title><title>Antimicrobial agents and chemotherapy</title><addtitle>Antimicrob Agents Chemother</addtitle><addtitle>Antimicrob Agents Chemother</addtitle><description>The proteasome is a promising target for antimalarial chemotherapy. We assessed
susceptibilities of fresh Plasmodium falciparum isolates from eastern Uganda to seven proteasome inhibitors: two asparagine ethylenediamines, two macrocyclic peptides, and three peptide boronates; five had median IC
values <100 nM. TDI8304, a macrocylic peptide lead compound with drug-like properties, had a median IC
of 16 nM. Sequencing genes encoding the β2 and β5 catalytic proteasome subunits, the predicted targets of the inhibitors, and five additional proteasome subunits, identified two mutations in β2 (I204T, S214F), three mutations in β5 (V2I, A142S, D150E), and three mutations in other subunits. The β2 S214F mutation was associated with decreased susceptibility to two peptide boronates, with IC
s of 181 nM and 2635 nM against mutant versus 62 nM and 477 nM against wild type parasites for MMV1579506 and MMV1794229, respectively, although significance could not be formally assessed due to the small number of mutant parasites with available data. The other β2 and β5 mutations and mutations in other subunits were not associated with susceptibility to tested compounds. Against culture-adapted Ugandan isolates, two asparagine ethylenediamines and the peptide proteasome inhibitors WLW-vinyl sulfone and WLL-vinyl sulfone (which were not studied
) demonstrated low nM activity, without decreased activity against β2 S214F mutant parasites. Overall, proteasome inhibitors had potent activity against P. falciparum isolates circulating in Uganda, and genetic variation in proteasome targets was uncommon.</description><subject>Antimalarials - chemistry</subject><subject>Antimalarials - pharmacology</subject><subject>Antimicrobial Chemotherapy</subject><subject>Asparagine</subject><subject>Drug Resistance - genetics</subject><subject>Ethylenediamines - pharmacology</subject><subject>Humans</subject><subject>Malaria, Falciparum - drug therapy</subject><subject>Malaria, Falciparum - parasitology</subject><subject>Mechanisms of Resistance</subject><subject>Peptides - pharmacology</subject><subject>Plasmodium falciparum - drug effects</subject><subject>Plasmodium falciparum - genetics</subject><subject>Proteasome Endopeptidase Complex - genetics</subject><subject>Proteasome Inhibitors - chemistry</subject><subject>Proteasome Inhibitors - pharmacology</subject><subject>Uganda</subject><issn>0066-4804</issn><issn>1098-6596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kU1LHTEUhkNpqbe2O9cyyxYce5LMZDIboYjWC0IF6zqcm5zRyMzkmmQK_ffGXpV20VW-Hp5D3pexAw7HnAv9FdEeA2je1UK8YSsOva5V26u3bAWgVN1oaPbYh5TuoZzbHt6zPamgbwRXK3Z9vSRL2-w3fvTZU6rCUN3c4uxwrq5GTFNwfpmqAUfrtxjLdp3CiLmQOVRXMWTCFCaq1vNdkeQQ00f2ruCJPj2v--zm_Ozn6UV9-eP7-vTbZY0N17nWpAYitSHpeskd8EFbUFKQtdpy3bmWFKKwDspd3-LgAJygloB30sJG7rOTnXe7bCZyluYccTTb6CeMv01Ab_59mf2duQ2_TN92ugFRBJ-fBTE8LJSymXxJYxxxprAkIzouJRcls4Ie7VAbQ0qRhtcxHMxTD6b0YP70YMST-csOLwEKcx-WOJck_sce_v2NV_FLSfIREk-TdA</recordid><startdate>20221018</startdate><enddate>20221018</enddate><creator>Garg, Shreeya</creator><creator>Kreutzfeld, Oriana</creator><creator>Chelebieva, Sevil</creator><creator>Tumwebaze, Patrick K</creator><creator>Byaruhanga, Oswald</creator><creator>Okitwi, Martin</creator><creator>Orena, Stephen</creator><creator>Katairo, Thomas</creator><creator>Nsobya, Samuel L</creator><creator>Conrad, Melissa D</creator><creator>Aydemir, Ozkan</creator><creator>Legac, Jennifer</creator><creator>Gould, Alexandra E</creator><creator>Bayles, Brett R</creator><creator>Bailey, Jeffrey A</creator><creator>Duffey, Maelle</creator><creator>Lin, Gang</creator><creator>Kirkman, Laura A</creator><creator>Cooper, Roland A</creator><creator>Rosenthal, Philip J</creator><general>American Society for Microbiology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0003-4085-5540</orcidid><orcidid>https://orcid.org/0000-0002-7953-7622</orcidid><orcidid>https://orcid.org/0000-0002-9984-8030</orcidid><orcidid>https://orcid.org/0000-0003-2026-345X</orcidid><orcidid>https://orcid.org/0000-0002-8437-9382</orcidid></search><sort><creationdate>20221018</creationdate><title>Susceptibilities of Ugandan Plasmodium falciparum Isolates to Proteasome Inhibitors</title><author>Garg, Shreeya ; 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We assessed
susceptibilities of fresh Plasmodium falciparum isolates from eastern Uganda to seven proteasome inhibitors: two asparagine ethylenediamines, two macrocyclic peptides, and three peptide boronates; five had median IC
values <100 nM. TDI8304, a macrocylic peptide lead compound with drug-like properties, had a median IC
of 16 nM. Sequencing genes encoding the β2 and β5 catalytic proteasome subunits, the predicted targets of the inhibitors, and five additional proteasome subunits, identified two mutations in β2 (I204T, S214F), three mutations in β5 (V2I, A142S, D150E), and three mutations in other subunits. The β2 S214F mutation was associated with decreased susceptibility to two peptide boronates, with IC
s of 181 nM and 2635 nM against mutant versus 62 nM and 477 nM against wild type parasites for MMV1579506 and MMV1794229, respectively, although significance could not be formally assessed due to the small number of mutant parasites with available data. The other β2 and β5 mutations and mutations in other subunits were not associated with susceptibility to tested compounds. Against culture-adapted Ugandan isolates, two asparagine ethylenediamines and the peptide proteasome inhibitors WLW-vinyl sulfone and WLL-vinyl sulfone (which were not studied
) demonstrated low nM activity, without decreased activity against β2 S214F mutant parasites. Overall, proteasome inhibitors had potent activity against P. falciparum isolates circulating in Uganda, and genetic variation in proteasome targets was uncommon.</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>36094216</pmid><doi>10.1128/aac.00817-22</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0003-4085-5540</orcidid><orcidid>https://orcid.org/0000-0002-7953-7622</orcidid><orcidid>https://orcid.org/0000-0002-9984-8030</orcidid><orcidid>https://orcid.org/0000-0003-2026-345X</orcidid><orcidid>https://orcid.org/0000-0002-8437-9382</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Antimalarials - chemistry Antimalarials - pharmacology Antimicrobial Chemotherapy Asparagine Drug Resistance - genetics Ethylenediamines - pharmacology Humans Malaria, Falciparum - drug therapy Malaria, Falciparum - parasitology Mechanisms of Resistance Peptides - pharmacology Plasmodium falciparum - drug effects Plasmodium falciparum - genetics Proteasome Endopeptidase Complex - genetics Proteasome Inhibitors - chemistry Proteasome Inhibitors - pharmacology Uganda |
| title | Susceptibilities of Ugandan Plasmodium falciparum Isolates to Proteasome Inhibitors |
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