Allergenic mites excrete cathepsins B and C as active cysteine proteases distinct from group 1 allergens

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00641049" target="_blank" >RIV/61388963:_____/25:00641049 - isvavai.cz</a>

Alternative codes found

RIV/00216208:11110/25:10506513

Result on the web

<a href="https://doi.org/10.1016/j.ijbiomac.2025.148383" target="_blank" >https://doi.org/10.1016/j.ijbiomac.2025.148383</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.ijbiomac.2025.148383" target="_blank" >10.1016/j.ijbiomac.2025.148383</a>

Result language

angličtina

Original language name

Allergenic mites excrete cathepsins B and C as active cysteine proteases distinct from group 1 allergens

Original language description

Allergenic mites are a major source of indoor allergens and are linked to the increasing prevalence of allergic diseases, posing a growing global health concern. Protease allergens released by mites play a key role in the development of hypersensitivity by disrupting the epithelial barrier and inducing immune responses through their proteolytic activity. In this study, we show that cysteine proteases significantly contribute to the overall proteolytic capacity of allergenic mites, particularly in house dust mites, and are involved in the degradation of human extracellular matrix proteins. Using a functional proteomics approach, combining specific substrates, inhibitors, and activity-based imaging probes, we profiled the component proteases in the species Dermatophagoides farinae and Acarus siro. This analysis identified two novel types of abundant, active cysteine proteases related to cathepsins: cathepsin B from D. farinae (DfCB) and cathepsin C from A. siro (AsCC), which are excreted into the environment via mite feces. Both cathepsins are clearly distinct from canonical cysteine proteases belonging to mite group 1 allergens, as demonstrated by comprehensive biochemical and functional characterizations, together with sequence and phylogenetic analyses. We also validated selective substrates for the detection of DfCB and AsCC in complex proteomes. Our findings suggest that DfCB and AsCC function as digestive enzymes in mites, and that their potent proteolytic activity, retained after excretion, may contribute to interactions with human tissues involved in allergic sensitization.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2025

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

International Journal of Biological Macromolecules

ISSN

0141-8130

e-ISSN

1879-0003

Volume of the periodical

331

Issue of the periodical within the volume

November

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

13

Pages from-to

148383

UT code for WoS article

001614985700006

EID of the result in the Scopus database

2-s2.0-105019929449