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Biology subjects

Colombo, M. I.

Publications and source records attributed to Colombo, M. I..

3 recordsLinked to original sources

Ursolic Acid Inhibits Rotavirus Replication Through Modulation Of Lipid Droplet Homeostasis

Rotavirus (RV) replication occurs within viroplasms (VP), which are globular, membrane-less cytosolic inclusions primarily assembled by the viral NSP5 and NSP2 proteins. Among host factors, lipid droplets (LD) are strictly required for VP biogenesis. LD are ubiquitous organelles consisting of a neutral lipid core surrounded by a phospholipid monolayer and associated proteins. Ursolic acid (UA), a pentacyclic triterpenoid widely present in plants and fruits, displays multiple biological activities, including modulation of lipid metabolism, and exhibits antiviral activity against RV, as we have previously demonstrated. Here, we investigated the molecular mechanism underlying the antiviral effect of UA. Using biophysical approaches, we first examined the impact of UA on LD formation, finding that it impairs LD biogenesis, consistent with reduced LD budding from the endoplasmic reticulum. We then employed cell-based assays to assess LD turnover and observed that UA acts as a lipolytic stimulus, leading to a marked reduction in LD abundance. Notably, we found that autophagic pathways contribute to LD degradation in the presence of UA. Finally, molecular dynamics simulations proposed that UA, owing to its intrinsic lipid-partitioning capacity, inserts into the LD phospholipid monolayer, establishing interactions with interdigitated neutral lipids. Together, our results indicate that UA both hampers LD biogenesis and accelerates LD degradation, likely through its association with and destabilization of the LD membrane. This dual effect leads to LD depletion, thereby impairing VP formation and ultimately inhibiting RV replication. IMPORTANCEDiarrheal diseases caused by a wide range of pathogens, including bacteria and viruses, remain a major global public health concern, accounting for more than one million deaths annually. These diseases mainly affect children under five years of age, with RV being the primary cause of diarrheal mortality in this age group. The burden is particularly severe in low- and middle-income countries. To address RV-associated disease, coordinated public health interventions have been implemented worldwide, including improvements in water, sanitation, hygiene, the introduction of vaccines, and the widespread use of oral rehydration therapy. Although these measures have substantially reduced the global burden of diarrheal diseases, the lack of a specific antiviral treatment against RV highlights the need for continued research. The development of antiviral strategies could provide a valuable complementary approach to existing interventions and help further reduce morbidity and mortality in infected children.

microbiology↗

Birnaviral Hijacking of Endosomal Membranes

Birnaviruses are a group of double-stranded RNA (dsRNA) viruses infecting birds, fish and insects. Early endosomes (EE) constitute the platform for viral replication. Here, we study the mechanism of birnaviral targeting of EE membranes. Using the Infectious Bursal Disease Virus (IBDV) as a model, we validate that the viral protein 3 (VP3) binds to phosphatidylinositol-3-phosphate (PI3P) present in EE membranes. We identify the domain of VP3 involved in PI3P-binding, named P2 and localized in the core of VP3, and establish the critical role of the arginine at position 200 (R200), conserved among all known birnaviruses. Mutating R200 abolishes viral replication. Moreover, we propose a two-stage modular mechanism for VP3 association with EE. Firstly, the carboxy-terminal region of VP3 adsorbs on the membrane, and then the VP3 core reinforces the membrane engagement by specifically binding PI3P through its P2 domain, additionally promoting PI3P accumulation. Significance StatementBirnaviruses are a family of viruses unique among the group of dsRNA viruses. Here, we show that VP3 seizes the endosomes by anchoring to the PI3P lipids in the luminal side of the EE membrane, in order to organize the viral replication factory. We propose a two-stage modular mechanism for VP3 association with PI3P-enriched EE. The significance of this work resides in the biochemical and biophysical insights on the mechanism of association of VP3 with EE and its role in the viral life cycle, which represents a substantial contribution toward understanding the replication strategy of these "non-canonical" viruses.

microbiology↗

Immunosuppressive role of PGE2 during human tuberculosis

Prostaglandin E2 (PGE2), an active lipid compound derived from arachidonic acid, regulates different stages of the immune response of the host during several pathologies such as chronic infections or cancer. Manipulation of PGE2 levels was proposed as an approach for countering the Type I IFN signature of tuberculosis (TB), but very limited information exists about this pathway in patients with active TB. Here, we demonstrated that PGE2 exerts a potent immunosuppressive action during the immune response of the human host against M. tuberculosis. Thus, we showed that PGE2 inhibited both lymphoproliferation and cytokine production of proinflammatory cytokines, together with a significant reduction of the surface expression of several immunological receptors in human cells. However, PGE2 promoted the autophagic flux of antigen-stimulated monocytes, even in the presence of IFN. In this way, the attenuation of inflammation and immunopathology caused by an excessive immune response emerges as an attractive therapeutic target. Together, our findings contribute to the knowledge of Mtb-resistance mediated by PGE2 and highlight the potential of this lipid mediator as a tool to improve anti-TB treatment.

immunology↗