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Lalle, M.

Publications and source records attributed to Lalle, M..

3 recordsLinked to original sources

Mechanistic insights into the activity of Benzoxaboroles against Cryptosporidium parvum: CPSF3 targeting and resistance implications

Benzoxaboroles are emerging as promising treatments against a broad range of protozoan parasites, including Trypanosoma, Leishmania, Plasmodium, Toxoplasma, and Cryptosporidium. We previously demonstrated that the benzoxaborole compound AN3661 inhibits the endonuclease activity of CPSF3 in Cryptosporidium hominis, likely by disrupting pre-mRNA processing, which in turn limits parasite growth. In this study, we further explored its mode of action and found that a specific mutation (Y385N) in CPSF3 of C. parvum confers strong resistance to AN3661. Interestingly, this mutation does not affect the parasites sensitivity to two other benzoxaboroles, AN13762 and AN7973, which are also thought to target CpCPSF3. All three compounds interfered with mRNA processing in C. parvum, consistent with inhibition of CPSF3 complex activity, and showed parasiticidal activity, especially during the late stages of merogony, blocking parasite egress. Two of them also impaired gamogony. In T. gondii, AN7973 remained effective against several strains carrying mutations within TgCPSF3 that confer resistance to AN3661 and AN13762, suggesting that it might represent an alternative chemotype targeting CPSF3 with the potential to overcome resistance. Notably, AN7973 successfully controlled severe infection in susceptible mice challenged with the AN3661-resistant C. parvum strain carrying the CpCPSF3Y385N mutation. Finally, we extended the known antiparasitic spectrum of AN3661 and AN7973 to include Eimeria tenella and Giardia duodenalis, two important pathogens in veterinary and human health. Altogether, our findings refine the understanding of CPSF3-targeting benzoxaboroles, identify alternative chemotypes with the potential to bypass resistance, and support their potential use in combination therapies to delay or prevent the emergence of drug resistance. Author summaryProtozoa are single-celled parasites that cause significant morbidity and mortality worldwide, affecting both humans and animals. The development of new targeted therapies with highly selective compounds requires a detailed understanding of their mode of action and precise interactions with parasite targets. Benzoxaboroles are a potent class of molecules active against Cryptosporidium, with compound AN3661 known to inhibit the endonuclease activity of the Cleavage and Polyadenylation Specificity Factor 3 (CPSF3) in Cryptosporidium hominis. Here, we show that this inhibitory effect is critical during both asexual and sexual developmental stages and that tyrosine at position 385 of C. parvum CPSF3 plays a key role in its inhibition. A mutation at this site confers resistance to AN3661 both in vitro and in vivo, but not to two other benzoxaboroles, AN13762 and AN7973. Notably, all three compounds disrupted pre-mRNA processing in Cryptosporidium, consistent with inhibition of the CPSF3 complex. Using Toxoplasma, a related protozoan that allows more efficient genetic manipulation, we found that none of the six mutations conferring resistance to compounds AN3661 and AN13762 conferred resistance to compound AN7973. AN7973, which strongly inhibits both C. parvum and T. gondii, may therefore represent an alternative chemotype targeting CPSF3. Furthermore, we demonstrated that the antiparasitic spectrum of AN3661and AN7973 extends to include E. tenella and G. duodenalis, two important pathogens in veterinary and human health. Altogether, our results refine the understanding of three CPSF3-targeting benzoxaboroles in Cryptosporidium and identify compound AN7973 as capable of overcoming resistance to AN3661, thereby supporting the rationale for combination therapies to prevent the emergence of drug resistance.

microbiology↗

High-resolution comparative atomic structures of two Giardiavirus prototypes infecting G.duodenalis parasite

Giardia lamblia virus (GLV) is a non-enveloped icosahedral dsRNA virus and an endosymbiont virus infecting the zoonotic protozoan parasite Giardia duodenalis (syn. G. lamblia, G. intestinalis), a pathogen of mammals, including humans. Elucidating the transmission mechanism of GLV is crucial to an in-depth understanding of the virulence of the virus in G. duodenalis. GLV belongs to the family Totiviridae, which infects yeast and protozoa intracellularly; however, it also transmits extracellularly, similar to phylogenetically distantly related toti-like viruses that infect multicellular hosts. The GLV capsid structure is extensively involved in the longstanding discussion concerning the acquisition of extracellular transmission in Totiviridae and toti-like viruses. Hence, this study constructed the first high-resolution comparative atomic models of two GLV strains, namely GLV-HP and GLV-CAT, which showed different intracellular localization and virulence phenotypes, using cryo-EM single-particle analysis. The atomic models of the GLV capsids presented swapped C-terminal extensions, extra surface loops, and a lack of cap-snatching pockets, similar to those of toti-like viruses. However, their open pores and lack of the extra crown protein (CrP) resemble those of other yeast and protozoan Totiviridae viruses, demonstrating the essential structures for acquiring extracellular cell-to-cell transmission. The intensive structural comparison between GLV-HP and GLV-CAT indicates the first evidence of critical structural motifs for the transmission and virulence of GLV in G. duodenalis.

biophysics↗

14-3-3 Negatively Regulates Actin Filament Formation In The Deep Branching Eukaryote Giardia lamblia

The phosphoserine/phosphothreonine-binding protein 14-3-3 is known to regulate actin, this function has been previously attributed to sequestration of phosphorylated cofilin. The deep branching eukaryote Giardia lamblia lacks cofilin and all other canonical actin-binding proteins (ABPs), and 14-3-3 was identified as an actin-associated protein in Giardia, yet its role in actin regulation was unknown. Gl14-3-3 depletion resulted in an overall disruption of actin organization characterized by ectopically distributed short actin filaments. Using phosphatase and kinase inhibitors, we demonstrated that actin phosphorylation correlated with destabilization of the actin network and increased complex formation with 14-3-3, while blocking actin phosphorylation stabilized actin filaments and attenuated complex formation. Giardia's sole Rho family GTPase, GlRac, modulates Gl14-3-3's association with actin, providing the first connection between GlRac and the actin cytoskeleton in Giardia. Giardia actin contains two putative 14-3-3 binding motifs, one of which (S330) is conserved in mammalian actin. Mutation of these sites reduced, but did not completely disrupt, the association with 14-3-3. Native gels and overlay assays indicate that intermediate proteins are required to support complex formation between 14-3-3 and actin. Overall, our results support a role for 14-3-3 as a negative regulator of actin filament formation.\n\nImportanceGiardia lacks canonical actin binding proteins. 14-3-3 was identified as an actin interactor but the significance of this interaction was unknown. Loss of 14-3-3 results in ectopic short actin filaments, indicating that 14-3-3 is an important regulator of the actin cytoskeleton in Giardia. Drug studies indicate that 14-3-3 complex formation is in part phospho-regulated. We demonstrate that complex formation is downstream of Giardias sole Rho family GTPase, GlRac, this result provides the first mechanistic connection between GlRac and actin in Giardia. Native gels and overlay assays indicate intermediate proteins are required to support the interaction between 14-3-3 and actin suggesting that 14-3-3 is regulating multiple actin complexes. Overall, we find that 14-3-3 is a negative regulator of actin filament formation in Giardia.

cell biology↗