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NOT Open Access | Changing Prevalence of Potential Mediators of Aminoquinoline, Antifolate, and Artemisinin Resistance Across Uganda

November 7, 2020 - 12:28 -- NOT Open Access
Asua V, Conrad MD, Rosenthal PJ, et al.
J Infect Dis. 2020 Nov 4:jiaa687

In Uganda artemether-lumefantrine is recommended for malaria treatment and sulfadoxine-pyrimethamine (SP) for chemoprevention during pregnancy, but drug resistance may limit efficacies.

Distribution pattern of amino acid mutations in chloroquine and antifolate drug resistance associated genes in complicated and uncomplicated Plasmodium vivax isolates from Chandigarh, North India

September 16, 2020 - 13:09 -- Open Access
Kaur H, Sehgal R, Kumar A, Bharti PK, Bansal D, Mohapatra PK, Mahanta J, Sultan AA
BMC Infect Dis. 2020 Sep 15;20(1):671

The increasing antimalarial drug resistance is a significant hindrance to malaria control and elimination programs. For the last six decades, chloroquine (CQ) plus pyrimethamine remains the first-line treatment for P. vivax malaria. Regions where both P. falciparum and P. vivax co-exist, P. vivax is exposed to antifolate drugs due to either misdiagnosis or improper treatment that causes selective drug pressure to evolve. Therefore, the present study aims to estimate antimalarial drug resistance among the complicated and uncomplicated P. vivax patients.

NOT Open Access | Antimalarial effect of cell penetrating peptides derived from the junctional region of Plasmodium falciparum dihydrofolate reductase-thymidylate synthase

July 20, 2020 - 15:20 -- NOT Open Access
Chaianantakul N, Sungkapong T, Supatip J, Kingsang P, Kamlaithong S, Suwanakitti N
Peptides. 2020 Jul 13:170372

Dihydrofolate reductase-thymidylate synthase of Plasmodium falciparum (PfDHFR-TS) is an important target of antifolate antimalarial drugs. However, drug resistant parasites are widespread in malaria endemic regions. The unique bifunctional property of PfDHFR-TS could be exploited for the design of allosteric inhibitors that interfere with the active dimer conformation. In this study, peptides were derived from the junctional region (JR) of PfDHFR-TS amino acid sequence in the αj1 helix (JR-helix) and the DHFR domain that is necessary for interaction with αj1 helix (JR21).

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