Dataset Information

Investigate the proteomic profiles of calf faecal extracellular vesicles: investigating gut health and infectious disease associated changes in calves

ABSTRACT: Faeces are considered easily accessible biological specimens that can be used to monitor gastrointestinal disorders. Extracellular vesicles (EVs) can be enriched from calf faeces, and these faecal extracellular vesicles (fEVs) consist of a diverse range of biological molecules, such as proteins, DNA, and RNA. The double membrane of EVs and the charged corona preserve their cargo, including proteins, from proteases, nucleases, and harsh environmental conditions. This enables the recovery of intact proteins secreted by the host and GI tract organisms, preserving their natural structure and function. While fEVs are suggested to mediate inter-species communication in the GI tract, the role of their protein cargo in GI infections remains unclear. Therefore, this study aimed to investigate the possibility of using fEVs as a non-invasive tool to investigate gut health and infections in claves. We considered Cryptosporidiosis as a model gut disease in calves to study the alteration in the proteomic profile of fEVs under gut infections.

INSTRUMENT(S):

ORGANISM(S): Bos Taurus (bovine)

TISSUE(S): Feces

SUBMITTER: Chanaka Premathilaka

LAB HEAD: Alireza Fazeli

PROVIDER: PXD068377 | Pride | 2026-01-23

REPOSITORIES: Pride

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Publications

Cryptosporidium spp. infection drives distinct alterations in the faecal extracellular vesicles metaproteome of calves.

Premathilaka Chanaka C Godakumara Kasun K Peffers Mandy Jayne MJ Clarke Emily J EJ Dorbek-Sundström Elisabeth E Orro Toomas T Kodithuwakku Suranga S Fazeli Alireza A

Journal of animal science and biotechnology 20260115 1

<h4>Background</h4>The gut is primarily responsible for digestion and nutrient absorption, plays essential roles in immune regulation and metabolic balance, and is supported by a diverse microbiome essential for digestion, absorption, and defence from pathogens. Understanding gut physiology and pathophysiology in pre-weaned calves is essential, as infections like cryptosporidiosis can lead to gut dysbiosis, impair growth, and negatively affect long-term productivity. Faeces are considered easily ...[more]

PMID: 41540478

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Project description:A heterobimetallic Mn/Fe cofactor is found in the R2 subunit of class Ic ribonucleotide reductases (R2c) and R2-like ligand-binding oxidases (R2lox). Although the protein-derived metal ligands are the same in both groups of proteins, the connectivity of the two metal ions and the chemistry each cofactor performs are different: in R2c, a one-electron oxidant, the Mn/Fe dimer is linked by two oxygen bridges (μ-oxo/μ-hydroxo), whereas in R2lox, a two-electron oxidant, it is linked by a single oxygen bridge (μ-hydroxo) and a fatty acid ligand. Here we identify a second coordination sphere residue which directs the divergent reactivity of the protein scaffold. The residue that directly precedes the N-terminal carboxylate metal ligand is conserved as a glycine within the R2lox group, but not in R2c. Mutation of the glycine to leucine converts the resting state R2lox cofactor into an R2c-like cofactor, a µ-oxo/µ-hydroxo bridged MnIII/FeIII dimer. This species has recently been observed as an intermediate of the oxygen activation reaction in wild-type R2lox, demonstrating that it is physiologically relevant. Cofactor maturation in R2c and R2lox therefore follows the same pathway, with structural and functional divergence of the two cofactor forms following oxygen activation. We also show that the leucine mutant no longer functions as a two-electron oxidant. Specifically the mass spectrometry data here deposited tracks the abundance of the cross-linked peptide AVIRAATVYNMIVE-AVTLD, which was used as surrogate marker for the abundance of the internal V72-Y162 ether cross-link, which is directly impacted by the metalation state of the protein as well as the residue present in position 68 (G or L). Taken together, our data demonstrate that the residue preceding the N-terminal metal ligand directs the cofactor’s reactivity towards one- or two-electron redox chemistry, presumably by setting the protonation state of the bridging oxygens and thereby perturbing the redox potential of the Mn ion.

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