Biology subjects

Cabrera, G.

Publications and source records attributed to Cabrera, G..

3 recordsLinked to original sources

bioRxiv2025

Detection of zoonotic Cryptosporidium parvum in invasive beavers from southern Tierra del Fuego, Chile

Since their introduction to Tierra del Fuego in 1946, invasive beavers have expanded their population and caused extensive environmental degradation across the subantarctic region. Beaver dams have profoundly impacted peatlands, mature sub-Antarctic forests, and watercourses. Here, we report a pathogen in invasive beavers in Patagonia and discuss their potential role as a reservoir of waterborne zoonotic pathogens. We detected Cryptosporidium through microscopy using the Ziehl-Neelsen staining technique in beaver collected from southern Tierra del Fuego. Out of the 105 beavers examined, three tested positive to optical microscopy, which were then identified molecularly as Cryptosporidium parvum by sequence analysis of the 18S ribosomal DNA (rDNA). Given the potential impacts of Cryptosporidium parvum upon native species, wildlife, and human health, this finding highlights the potential risks associated with the ongoing expansion of beavers into other areas of the sub-Antarctic region. A potential role of invasive beavers as reservoirs of zoonotic Cryptosporidium spp. in Patagonia emphasizes the unknown consequences of human-introduced exotic species on pristine ecosystems.

bioengineering↗

bioRxiv2024

Structural and Functional Glycosylation of the Abdala COVID-19 Vaccine

Abdala is a COVID-19 vaccine produced in Pichia pastoris and is based on the receptor-binding domain (RBD) of the SARS-CoV-2 spike. Abdala is currently approved for use in multiple countries with clinical trials confirming its safety and efficacy in preventing severe illness and death. Although P. pastoris is used as an expression system for protein-based vaccines, yeast glycosylation remains largely uncharacterised across immunogens. Here, we characterise N-glycan structures and their site of attachment on Abdala and show how yeast-specific glycosylation decreases binding to the ACE2 receptor and a receptor-binding motif (RBM) targeting antibody compared to the equivalent mammalian-derived RBD. Reduced receptor and antibody binding is attributed to changes in conformational dynamics resulting from N-glycosylation. These data highlight the critical importance of glycosylation in vaccine design and demonstrate how individual glycans can influence host interactions and immune recognition via protein structural dynamics.

biochemistry↗

bioRxiv2021

In-solution buffer-free digestion for the analysis of SARS-CoV-2 RBD proteins allows a full sequence coverage and detection of post-translational modifications in a single ESI-MS spectrum

Subunit vaccines based on the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2, are among the most promising strategies to fight the COVID-19 pandemic. The detailed characterization of the protein primary structure by mass spectrometry (MS) is mandatory, as described in ICHQ6B guidelines. In this work, several recombinant RBD proteins produced in five expression systems were characterized using a non-conventional protocol known as in-solution buffer-free digestion (BFD). In a single ESI-MS spectrum, BFD allowed very high sequence coverage ([≥] 99 %) and the detection of highly hydrophilic regions, including very short and hydrophilic peptides (2-8 amino acids), the His6-tagged C-terminal peptide carrying several post-translational modifications at Cys538 such as cysteinylation, glutathionylation, cyanilation, among others. The analysis using the conventional digestion protocol allowed lower sequence coverage (80-90 %) and did not detect peptides carrying some of the above-mentioned post-translational modifications. The two C-terminal peptides of a dimer [RBD(319-541)-(His)6]2 linked by an intermolecular disulfide bond (Cys538-Cys538) with twelve histidine residues were only detected by BFD. This protocol allows the detection of the four disulfide bonds present in the native RBD and the low-abundance scrambling variants, free cysteine residues, O-glycoforms and incomplete processing of the N-terminal end, if present. Artifacts that might be generated by the in-solution BFD protocol were also characterized. BFD can be easily implemented and we foresee that it can be also helpful to the characterization of mutated RBD.

biochemistry↗