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Table 1 Bacteria and bacterial products that activate the ER stress sensors

From: Diverse roles of endoplasmic reticulum stress sensors in bacterial infection

Bacterium Virulence factor Cell type UPR-specific host response Mechanism Reference
IRE1 PERK ATF6
Aeromonas hydrophila Aerolysin HeLa XBP1-s n.d. n.d.   [3]
Bacillus thuringiensis Cry5B C. elegans xbp1-s n.d. n.d. p38 [3]
Brucella abortus   BMM xbp1-s n.d. n.d.   [16]
Chlamydia pneumoniae   HEp-2 eIF2α-p Persistent infection [13]
Francisella tularensis   BMM xbp1-s n.d. n.d. TLR2 [8]
Gram-negative bacteria LPS Monocytic THP-1 XBP1-s PERK-p, eIF2α-p ATF6 cleavage TLR4 [2]
Helicobacter pylori HP0175 AGS n.d. PERK-p, CHOP, ATF4, eIF2α-p n.d.   [23]
Legionella pneumophila   BMM, HEK-293 FCγ, RAW264.7 Block of xbp1-s Block of CHOP translation ATF6 cleavage   [14]
Listeria monocytogenes LLO P388D1, HeLa xbp1-s eIF2α-p ATF6 cleavage   [5]
Mycobacterium tuberculosis ESAT-6 A549 xbp1-s eIF2α-p, ATF4, chop n.d. ER Ca2+ release, ROS [4]
Pseudomonas aeruginosa   C. elegans xbp1-s n.d. n.d. PMK-1 (p38 orthologue) [7]
Shigella dysenteriae, STEC Stx1 Monocytic THP-1 IRE1, xbp1-s PERK-p, chop ATF6 cleavage Unfolded Stx (not for IRE1) [9]
Macrophage-like THP-1 IRE1-p, xbp1-s PERK-p, CHOP Unfolded Stx [12]
Staphylococcus aureus   BMM, RAW264.7 xbp1-s n.d. n.d. TLR2/4/9 [17]
STEC SubAB Vero, MEF xbp1-s chop, eIF2α-p, atf4 ATF6 cleavage BiP cleavage [10]
Streptococcus pneumoniae H2O2 H441 decrease of xbp1-s PERK-p, atf4, eIF2α-p, atf3, chop ROS [6]
Streptomyces sp. Tunicamycin P388D1, HeLa, C. elegans, J774 xbp1-s, IRE1-p PERK-p, chop ATF6 cleavage Inhibition of N-linked glycosylation [5, 7, 8]
Vibrio cholerae CT T84 IRE1-p,
xbp1-s
Interaction with IRE1 [11]
Yersinia pseudotuberculosis   MEF, RAW264.7 n.d. eIF2α-p, atf3 n.d.   [21]