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Gingipain regulates isoform switches of PD-L1 in macrophages infected with Porphyromonas gingivalis
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Gingipain regulates isoform switches of PD-L1 in macrophages infected with Porphyromonas gingivalis
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Gingipain regulates isoform switches of PD-L1 in macrophages infected with Porphyromonas gingivalis
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Journal Article
Gingipain regulates isoform switches of PD-L1 in macrophages infected with Porphyromonas gingivalis
2025
Overview
Periodontal pathogen
Porphyromonas gingivalis
(
P. gingivalis
) is believed to possess immune evasion capabilities, but it remains unclear whether this immune evasion is related to host gene alternative splicing (AS). In this study, RNA-sequencing revealed significant changes in both AS landscape and transcriptomic profile of macrophages following
P. gingivalis
infection with/without knockout of gingipain (a unique toxic protease of
P. gingivalis
).
P. gingivalis
infection increased the PD-L1 transcripts expression and selectively upregulated a specific coding isoform that more effectively binds to PD-1 on T cells, thereby inhibiting immune function. Biological experiments also detected AS switch of PD-L1 in
P. gingivalis
-infected or gingipain-treated macrophages. AlphaFold 3 predictions indicated that the protein docking compatibility between PD-1 and
P. gingivalis
-upregulated PD-L1 isoform was over 80% higher than another coding isoform. These findings suggest that
P. gingivalis
employs gingipain to modulate the AS of PD-L1, facilitating immune evasion.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 631/326
/ Animals
/ Bacteroidaceae Infections - genetics
/ Bacteroidaceae Infections - immunology
/ Bacteroidaceae Infections - metabolism
/ Bacteroidaceae Infections - microbiology
/ Gingipain Cysteine Endopeptidases - genetics
/ Gingipain Cysteine Endopeptidases - metabolism
/ Humanities and Social Sciences
/ Humans
/ Ligands
/ Mice
/ PD-L1
/ Porphyromonas gingivalis - pathogenicity
/ Protein Isoforms - metabolism
/ Proteins
/ Science
