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A Effector with Enhanced Inhibitory
Activity on the NF-κB Pathway Activates the NLRP3/ASC/Caspase-1 Inflammasome
in Macrophages


A type III secretion system (T3SS) in pathogenic Yersinia

species functions to translocate Yop effectors, which modulate cytokine

production and regulate cell death in macrophages. Distinct pathways of

T3SS-dependent cell death and caspase-1 activation occur in

Yersinia-infected macrophages. One pathway of cell death

and caspase-1 activation in macrophages requires the effector YopJ. YopJ is an

acetyltransferase that inactivates MAPK kinases and IKKβ to cause

TLR4-dependent apoptosis in naïve macrophages. A YopJ isoform in Y.

pestis
KIM (YopJKIM) has two amino acid substitutions,

F177L and K206E, not present in YopJ proteins of Y.

pseudotuberculosis
and Y. pestis CO92. As compared

to other YopJ isoforms, YopJKIM causes increased apoptosis, caspase-1

activation, and secretion of IL-1β in Yersinia-infected

macrophages. The molecular basis for increased apoptosis and activation of

caspase-1 by YopJKIM in Yersinia-infected

macrophages was studied. Site directed mutagenesis showed that the F177L and

K206E substitutions in YopJKIM were important for enhanced apoptosis,

caspase-1 activation, and IL-1β secretion. As compared to

YopJCO92, YopJKIM displayed an enhanced capacity to

inhibit phosphorylation of IκB-α in macrophages and to bind IKKβ in

vitro. YopJKIM also showed a moderately increased ability to inhibit

phosphorylation of MAPKs. Increased caspase-1 cleavage and IL-1β secretion

occurred in IKKβ-deficient macrophages infected with Y.

pestis
expressing YopJCO92, confirming that the

NF-κB pathway can negatively regulate inflammasome activation.

K+ efflux, NLRP3 and ASC were important for secretion of

IL-1β in response to Y. pestis KIM infection as shown using

macrophages lacking inflammasome components or by the addition of exogenous KCl.

These data show that caspase-1 is activated in naïve macrophages in

response to infection with a pathogen that inhibits IKKβ and MAPK kinases

and induces TLR4-dependent apoptosis. This pro-inflammatory form of apoptosis

may represent an early innate immune response to highly virulent pathogens such

as Y. pestis KIM that have evolved an enhanced ability to

inhibit host signaling pathways.


Vyšlo v časopise: A Effector with Enhanced Inhibitory Activity on the NF-κB Pathway Activates the NLRP3/ASC/Caspase-1 Inflammasome in Macrophages. PLoS Pathog 7(4): e32767. doi:10.1371/journal.ppat.1002026
Kategorie: Research Article
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.ppat.1002026

Souhrn

A type III secretion system (T3SS) in pathogenic Yersinia

species functions to translocate Yop effectors, which modulate cytokine

production and regulate cell death in macrophages. Distinct pathways of

T3SS-dependent cell death and caspase-1 activation occur in

Yersinia-infected macrophages. One pathway of cell death

and caspase-1 activation in macrophages requires the effector YopJ. YopJ is an

acetyltransferase that inactivates MAPK kinases and IKKβ to cause

TLR4-dependent apoptosis in naïve macrophages. A YopJ isoform in Y.

pestis
KIM (YopJKIM) has two amino acid substitutions,

F177L and K206E, not present in YopJ proteins of Y.

pseudotuberculosis
and Y. pestis CO92. As compared

to other YopJ isoforms, YopJKIM causes increased apoptosis, caspase-1

activation, and secretion of IL-1β in Yersinia-infected

macrophages. The molecular basis for increased apoptosis and activation of

caspase-1 by YopJKIM in Yersinia-infected

macrophages was studied. Site directed mutagenesis showed that the F177L and

K206E substitutions in YopJKIM were important for enhanced apoptosis,

caspase-1 activation, and IL-1β secretion. As compared to

YopJCO92, YopJKIM displayed an enhanced capacity to

inhibit phosphorylation of IκB-α in macrophages and to bind IKKβ in

vitro. YopJKIM also showed a moderately increased ability to inhibit

phosphorylation of MAPKs. Increased caspase-1 cleavage and IL-1β secretion

occurred in IKKβ-deficient macrophages infected with Y.

pestis
expressing YopJCO92, confirming that the

NF-κB pathway can negatively regulate inflammasome activation.

K+ efflux, NLRP3 and ASC were important for secretion of

IL-1β in response to Y. pestis KIM infection as shown using

macrophages lacking inflammasome components or by the addition of exogenous KCl.

These data show that caspase-1 is activated in naïve macrophages in

response to infection with a pathogen that inhibits IKKβ and MAPK kinases

and induces TLR4-dependent apoptosis. This pro-inflammatory form of apoptosis

may represent an early innate immune response to highly virulent pathogens such

as Y. pestis KIM that have evolved an enhanced ability to

inhibit host signaling pathways.


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Štítky
Hygiena a epidemiológia Infekčné lekárstvo Laboratórium

Článok vyšiel v časopise

PLOS Pathogens


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