Biology subjects

Veloso, T.

Publications and source records attributed to Veloso, T..

3 recordsLinked to original sources

bioRxiv2026

SpaceBio Knowledge Hub: A LiteratOmics Platform for Microgravity and Space Biology Research

Space biology literature is growing exponentially. Existing infrastructure has not kept pace with organizing, synthesizing, and disseminating this knowledge. We present SpaceBio SpaceBio Knowledge Hub (www.spacebio.space), an integrated digital ecosystem that combines artificial intelligence, real-time data integration, and open-access infrastructure to advance research, education, and collaboration in microgravity, space biology and space exploration. The platform applies AI-driven approaches including natural language processing, machine learning, and automated content generation to construct a semantic atlas of the field. The atlas reveals the hierarchical thematic organization underlying microgravity-induced biological responses, space mission infrastructure, planetary science, and astrobiology. As part of this effort, SpaceBio is moving toward the construction of a LiteratOmics framework for microgravity, and space biology a systematic, AI-enabled approach to mining, integrating, and structuring the primary literature generated by omics-driven spaceflight research, treating the scientific literature itself as a navigable data layer alongside genomic, transcriptomic, and proteomic datasets. Built on a scalable, cloud-based architecture with a user-centered interface, SpaceBio supports literature exploration, data integration, and knowledge discovery for researchers, educators, students, industry partners, and citizen scientists. The platform also functions as a community-building ecosystem. It integrates hands-on research initiatives, AI-generated educational content, pilot data science projects, and social responsibility programs that broaden participation without compromising scientific rigor. AI-enabled digital environments can transform fragmented literature into a navigable knowledge landscape. SpaceBio accelerates research productivity, strengthens STEM education, and supports the global space life sciences community as human space exploration enters in the most ambitious era.

scientific communication and education↗

bioRxiv2024

Dynamic ensembles of SARS-CoV-2 N-protein reveal head-to-head coiled-coil-driven oligomerization and phase separation

The SARS-CoV-2 nucleocapsid (N) protein is essential for the viral lifecycle, facilitating RNA packaging, replication, and host-cell interactions. Its ability to self-assemble and undergo liquid-liquid phase separation (LLPS) is critical for these functions but remains poorly understood. Using an integrated approach combining small-angle X-ray scattering (SAXS), nuclear magnetic resonance (NMR) spectroscopy, computational modeling, and biophysical assays, we uncover key mechanisms underpinning N-proteins dynamic self-assembly. We show that the N-proteins interdomain linker (IDL) contains a conserved coiled-coil (CC) motif that drives transient interactions between protein subunits, enabling the formation of progressively larger complexes at higher concentrations. SAXS analysis and ensemble modeling reveal that the IDL exists in a concentration-dependent equilibrium between monomeric, dimeric, and trimeric states. The CC motif facilitates parallel, head-to-head oligomerization of N-protein dimers, transitioning between compact (closed) and extended (open) configurations depending on the interaction network within the IDL. This linker-driven assembly modulates LLPS, impacting the size, stability, and dynamics of biomolecular condensates. Here, we present the most comprehensive conformational landscape analysis of the N-protein to date, providing a detailed model of its self-assembly and LLPS. Our findings highlight how the structural plasticity of the IDL and CC-mediated interactions are pivotal to its roles in the SARS-CoV-2 lifecycle.

biophysics↗

bioRxiv2021

A pathogen-encoded signaling receptor mediating host-like interactions through intrinsic disorder

The translocated intimin receptor (Tir) is a central effector of Attaching and Effacing (A/E) pathogens responsible for worldwide foodborne disease cases. Tir acts as a cell-surface receptor in host cells, rewiring intracellular processes to assist infection by targeting multiple host proteins. We sought to understand the basis for Tir binding diversity in signaling. Here, we establish that Tir is a disordered protein with host-like binding motifs. A trait we find prevalent in several other effectors secreted by A/E bacteria. We disclose that Tir has a disordered C-terminal intracellular tail (C-Tir) with non-random structural preferences at phosphorylation sites, including host-like tyrosine-based motifs, with versatile lipid- and SH2 domain binding capability pre-phosphorylation. We show that multi-site tyrosine phosphorylation enables C-Tir to engage SH2 domains in a multivalent manner, consistent with Tirs scaffold/hub role for host proteins. Last, we uncover Tirs ability to dimerizes via its partially disordered N-terminal intracellular domain. Collectively, our findings provide an updated picture of Tirs intracellular side, highlighting its ability to mimic host disordered membrane receptors versatility as a molecular strategy for host evasion. SummaryTir is a cell-surface receptor secreted by life-threatening pathogens. Upon delivery into host cells, Tir inserts the host plasma membrane providing a means for these extracellular pathogens to control host intracellular processes. To prevent pathogens from relying on Tir, it is essential to understand its intracellular mechanics. This paper provides a coherent picture of the intracellular side of Tir, highlighting its ability to copycat the interactions of disordered intracellular domains of host immune receptors. This copycatting allows the bacterial pathogens to modulate critical host processes, allowing infection to spread further without triggering the immune system response. This work proposes that other bacterial secreted pathogenic proteins exploit intrinsic disorder to hijack human cells, suggesting a widespread host subversion mechanism.

biophysics↗