Table 1.

Bacteria and bacterial products that activate the ER stress sensors

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]