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Biology subjects

Touarin, P.

Publications and source records attributed to Touarin, P..

2 recordsLinked to original sources

Molecular and functional dissection of the AP2-I/BDP1 transcriptional complex of the malaria parasite reveals a role beyond the red blood cell stages

The transcription factor AP2-I and the bromodomain protein BDP1 of the malaria parasite bind upstream of several genes implicated in red blood cell invasion. Here, we demonstrate that they form a complex and that AP2-I recruits BDP1 to the target genes. The ACDC domain of AP2-I interacts with a BDP1 region called BAAS, located between the ankyrin and the bromodomain. The ankyrin, in turn, binds to a conserved AP2-I specific region called ASAIR. Three of the interacting domains are parasite-specific, allowing inhibition without affecting the host. We further show that AP2-I is essential for asexual blood stage development, playing multiple roles, and that AP2-I and BDP1 function beyond invasion, binding to the promoters of the gametocytogenesis regulators gdv1 and ap2-g, suggesting a role for the AP2-I/BDP1 complex in parasite sexual commitment. Overall, our study highlights the essential and unique nature of the AP2-I/BDP1 complex and its potential as a novel antimalarial drug target. Author summaryThe transcription factor AP2-I and the bromodomain protein BDP1 of the malaria parasite have previously been shown to be implicated in red blood cell invasion by the human malaria parasite. Here we show that they form a complex and identify the interacting domains on each protein. Three of these are parasite-specific, allowing inhibition without affecting the human host. We also show that AP2-I is essential for parasite survival in the blood and that the protein is implicated in other processes beyond red blood cell invasion. Namely, AP2-I, but also BDP1, bind to the promoters of the gametocytogenesis regulators gdv1 and ap2-g, suggesting a role for the AP2-I/BDP1 complex in parasite sexual commitment, without which the parasite cannot be transmitted.

microbiology↗

Pre-B cell receptor acts as a selectivity switch for Galectin-1 at the pre-B cell surface

Galectins are glycan binding proteins translating the sugar-encoded information of cellular glycoconjugates into many physiological activities including immunity, cell migration, and signaling. During early B lymphocytes (BL) development at the pre-B cell stage, BL express the pre-B cell receptor (pre-BCR) and are supported by mesenchymal stromal cells secreting Galectin-1 (Gal-1). Gal-1 interacts with glycosylated receptors from stromal and pre-B cell surfaces but also with the pre-BCR through a direct carbohydrate-independent contact. How this interaction might interplay with the glycan-decoding function of Gal-1 is unknown. Here, we investigated Gal-1 binding to cell surface ligands using NMR spectroscopy on native membranes. We showed that pre-BCR regulates Gal-1 binding to specifically target 2,3-sialylated receptors on pre-B cells. Upon pre-BCR interaction, dynamic changes resulted in additional contacts with 2,3-sialylated glycans converting Gal-1 from an exo- to an endo-type lectin. Remarkably, this selectivity switch is able to promote pre-B cell survival. Altogether, we shed light on a new mechanism allowing fine-tuning of Galectin specificity at the cell surfaces.

biochemistry↗