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

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]