About: Non‐proteolytic functions of microbial proteases increase pathological complexity

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An Entity of Type : schema:ScholarlyArticle, within Data Space : covidontheweb.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Non‐proteolytic functions of microbial proteases increase pathological complexity
Creator	Djordjevic, Steven Jarocki, Veronica Tacchi, Jessica
source	Medline; PMC
abstract	Proteases are enzymes that catalyse hydrolysis of peptide bonds thereby controlling the shape, size, function, composition, turnover and degradation of other proteins. In microbes, proteases are often identified as important virulence factors and as such have been targets for novel drug design. It is emerging that some proteases possess additional non‐proteolytic functions that play important roles in host epithelia adhesion, tissue invasion and in modulating immune responses. These additional “moonlighting” functions have the potential to obfuscate data interpretation and have implications for therapeutic design. Moonlighting enzymes comprise a subcategory of multifunctional proteins that possess at least two distinct biological functions on a single polypeptide chain. Presently, identifying moonlighting proteins relies heavily on serendipitous empirical data with clues arising from proteins lacking signal peptides that are localised to the cell surface. Here, we describe examples of microbial proteases with additional non‐proteolytic functions, including streptococcal pyrogenic exotoxin B, PepO and C5a peptidases, mycoplasmal aminopeptidases, mycobacterial chaperones and viral papain‐like proteases. We explore how these non‐proteolytic functions contribute to host cell adhesion, modulate the coagulation pathway, assist in non‐covalent folding of proteins, participate in cell signalling, and increase substrate repertoire. We conclude by describing how proteomics has aided in moonlighting protein discovery, focusing attention on potential moonlighters in microbial exoproteomes.
has issue date	2015-02-06(xsd:dateTime)
bibo:doi	10.1002/pmic.201400386
bibo:pmid	25492846
has license	no-cc
sha1sum (hex)	ad4f88e2fe4359bf084a954cc9fa73280e83b1d3
schema:url	https://doi.org/10.1002/pmic.201400386
resource representing a document's title	Non‐proteolytic functions of microbial proteases increase pathological complexity
has PubMed Central identifier	PMC7167786
has PubMed identifier	25492846
schema:publication	Proteomics
resource representing a document's body	covid:ad4f88e2fe4359bf084a954cc9fa73280e83b1d3#body_text
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