Endogenous pore-forming protein complex targets acidic glycosphingolipids in lipid rafts to initiate endolysosome regulation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2019-12

AUTHORS

Xiao-Long Guo, Ling-Zhen Liu, Qi-Quan Wang, Jin-Yang Liang, Wen-Hui Lee, Yang Xiang, Sheng-An Li, Yun Zhang

ABSTRACT

Bacterial pore-forming toxin aerolysin-like proteins (ALPs) are widely distributed in animals and plants. However, functional studies on these ALPs remain in their infancy. βγ-CAT is the first example of a secreted pore-forming protein that functions to modulate the endolysosome pathway via endocytosis and pore formation on endolysosomes. However, the specific cell surface molecules mediating the action of βγ-CAT remain elusive. Here, the actions of βγ-CAT were largely attenuated by either addition or elimination of acidic glycosphingolipids (AGSLs). Further study revealed that the ALP and trefoil factor (TFF) subunits of βγ-CAT bind to gangliosides and sulfatides, respectively. Additionally, disruption of lipid rafts largely impaired the actions of βγ-CAT. Finally, the ability of βγ-CAT to clear pathogens was attenuated in AGSL-eliminated frogs. These findings revealed a previously unknown double binding pattern of an animal-secreted ALP in complex with TFF that initiates ALP-induced endolysosomal pathway regulation, ultimately leading to effective antimicrobial responses. More... »

PAGES

59

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s42003-019-0304-y

DOI

http://dx.doi.org/10.1038/s42003-019-0304-y

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1112057682

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/30775460


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