The Open UniversitySkip to content
 

Deiminated proteins in extracellular vesicles and serum of llama (Lama glama)—Novel insights into camelid immunity

Criscitiello, Michael F.; Kraev, Igor and Lange, Sigrun (2020). Deiminated proteins in extracellular vesicles and serum of llama (Lama glama)—Novel insights into camelid immunity. Molecular Immunology, 117 pp. 37–53.

DOI (Digital Object Identifier) Link: https://doi.org/10.1016/j.molimm.2019.10.017
Google Scholar: Look up in Google Scholar

Abstract

Peptidylarginine deiminases (PADs) are phylogenetically conserved calcium-dependent enzymes which post-translationally convert arginine into citrulline in target proteins in an irreversible manner, causing functional and structural changes in target proteins. Protein deimination causes generation of neo-epitopes, affects gene regulation and also allows for protein moonlighting. Furthermore, PADs have been found to be a phylogenetically conserved regulator for extracellular vesicle (EVs) release. EVs are found in most body fluids and participate in cellular communication via transfer of cargo proteins and genetic material. In this study, post-translationally deiminated proteins in serum and serum-EVs are described for the first time in camelids, using the llama (Lama glama L. 1758) as a model animal. We report a poly-dispersed population of llama serum EVs, positive for phylogenetically conserved EV-specific markers and characterised by TEM. In serum, 103 deiminated proteins were overall identified, including key immune and metabolic mediators including complement components, immunoglobulin-based nanobodies, adiponectin and heat shock proteins. In serum, 60 deiminated proteins were identified that were not in EVs, and 25 deiminated proteins were found to be unique to EVs, with 43 shared deiminated protein hits between both serum and EVs. Deiminated histone H3, a marker of neutrophil extracellular trap formation, was also detected in llama serum. PAD homologues were identified in llama serum by Western blotting, via cross reaction with human PAD antibodies, and detected at an expected 70 kDa size. This is the first report of deiminated proteins in serum and EVs of a camelid species, highlighting a hitherto unrecognized post-translational modification in key immune and metabolic proteins in camelids, which may be translatable to and inform a range of human metabolic and inflammatory pathologies.

Item Type: Journal Item
Copyright Holders: 2019 Elsevier Ltd.
ISSN: 0161-5890
Keywords: Peptidylarginine deiminases (PADs); Protein deimination; Llama (<i>Lama glama</i>); extracellular vesicles (EVs); Innate immunity; Adaptive immunity; Metabolism; Complement; Nanobodies; Immunoglobulin; Adiponectin; Histone
Academic Unit/School: Faculty of Science, Technology, Engineering and Mathematics (STEM)
Related URLs:
Item ID: 68217
Depositing User: ORO Import
Date Deposited: 21 Nov 2019 09:56
Last Modified: 09 Dec 2019 11:18
URI: http://oro.open.ac.uk/id/eprint/68217
Share this page:

Metrics

Altmetrics from Altmetric

Citations from Dimensions

Actions (login may be required)

Policies | Disclaimer

© The Open University   contact the OU