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Louvat, C.

Publications and source records attributed to Louvat, C..

3 recordsLinked to original sources

AP2-L-Dependent Processes Promote PVM Maintenance and Plasmodium Liver-stage Development

Successful malaria infection requires transformation of Plasmodium sporozoites into replicative exo-erythrocytic forms (EEFs) within hepatocytes, a process requiring a functional parasitophorous vacuole membrane (PVM) and interactions with host cellular pathways. ApiAP2 transcription factors regulate developmental progression throughout the Plasmodium life cycle. AP2-L consists of an extended amino terminal region and two AP2 domains and is highly expressed in asexual stage trophozoites, sporozoites and early EEFs, but its role in these stages is poorly understood. We characterized the functional consequences of deleting the entire P. berghei ap2-l coding sequence on the erythrocytic cycle in vivo, sporozoite gene expression, liver-stage development, and hepatocyte-parasite interactions. AP2L-KO parasites maintained erythrocytic replication but sporozoite inoculation failed to establish blood-stage infection in mice. AP2-L loss decreased transcripts encoding proteins involved in sporozoite gliding motility, host-cell entry, and rhoptry secretion. Motif discovery upstream of a subset of these genes suggests possible direct targets of AP2-L. Infected HepG2 cells showed reduced EEF numbers and sizes, impaired parasite DNA replication, and abnormal parasite positioning relative to the host nucleus. PVMs of AP2L-KO parasites exhibited aberrant localization of proteins, absence of tubular vacuolar network extensions, and sensitivity to detergent. These abnormalities were accompanied by increased accumulation of the host's autophagy-associated protein around parasites, suggesting efficient host-mediated elimination. Additionally, AP2L-KO parasites displayed reduced association with the host microtubule-organizing center, Golgi compartments, and COPB2-positive vesicular structures, suggesting an impairment in uptake of nutrients. Together, these findings demonstrate that AP2-L directs both vacuolar biogenesis and host cytoskeletal/vesicular capture in liver-stage parasites.

microbiology↗

Stable Structures or poly(A)-binding protein loading protect cellular and viral RNAs against ISG20-mediated decay

ISG20 is an interferon-induced 3-to-5 RNA exonuclease that acts as a broad antiviral factor. At present, the features that expose RNA to ISG20 remain unclear, although recent studies have pointed to the modulatory role of epitranscriptomic modifications in the susceptibility of target RNAs to ISG20. These findings raise the question as to how cellular RNAs, on which these modifications are abundant, cope with ISG20. To obtain an unbiased perspective on this topic, we used RNAseq and biochemical assays to identify elements that regulate the behavior of RNAs against ISG20. The results we have obtained indicate that poly(A)-binding protein (PABP1) loading on the RNA 3 tail provides a primal protection against ISG20, easily explaining the overall protection of cellular mRNAs observed by RNAseq. The second element we uncovered is provided by terminal stem-loop RNA structures, that have been associated to ISG20 protection before, but that we re-examine here systematically to define the stabilities that tilt the balance between resistance and susceptibility to ISG20. Given that these elements are present on cellular mRNAs, but can be co-opted by viruses as well, these results shed new light on the complex interplay that regulates the susceptibility of different classes of viruses against ISG20.

microbiology↗

The HIV-1 Integrase C-Terminal domain induces TAR RNA structural changes promoting Tat binding.

Recent evidence indicated that HIV-1 Integrase (IN) binds genomic viral RNA (gRNA) playing a critical role in viral particle morphogenesis and gRNA stability in host cells. Combining biophysical and biochemical approaches we show that the C-terminal flexible 18-residues tail of IN acts as a sensor of the peculiar apical structure of trans-activation response element RNA (TAR), directly interacting with its hexaloop. We highlighted how the whole IN C-terminal domain, once bound to TAR, can change its structure assisting the binding of Tat, the HIV trans-activator protein, which finally displaces IN from TAR. Our results are consistent with the emerging role of IN in early stage of proviral transcription and suggest new steps of HIV-1 life cycle that can be considered as therapeutic targets.

biochemistry↗