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

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/00216208:11110/25:10506513

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

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

Název periodika

International Journal of Biological Macromolecules

ISSN

0141-8130

e-ISSN

1879-0003

Svazek periodika

331

Číslo periodika v rámci svazku

November

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

13

Strana od-do

148383

Kód UT WoS článku

001614985700006

EID výsledku v databázi Scopus

2-s2.0-105019929449