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2016 ; 84
(6
): 1796-1805
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The Tick Protein Sialostatin L2 Binds to Annexin A2 and Inhibits NLRC4-Mediated
Inflammasome Activation
#MMPMID27045038
Wang X
; Shaw DK
; Sakhon OS
; Snyder GA
; Sundberg EJ
; Santambrogio L
; Sutterwala FS
; Dumler JS
; Shirey KA
; Perkins DJ
; Richard K
; Chagas AC
; Calvo E
; Kopecký J
; Kotsyfakis M
; Pedra JHF
Infect Immun
2016[Jun]; 84
(6
): 1796-1805
PMID27045038
show ga
Tick saliva contains a number of effector molecules that inhibit host immunity
and facilitate pathogen transmission. How tick proteins regulate immune
signaling, however, is incompletely understood. Here, we describe that loop 2 of
sialostatin L2, an anti-inflammatory tick protein, binds to annexin A2 and
impairs the formation of the NLRC4 inflammasome during infection with the
rickettsial agent Anaplasma phagocytophilum Macrophages deficient in annexin A2
secreted significantly smaller amounts of interleukin-1? (IL-1?) and IL-18 and
had a defect in NLRC4 inflammasome oligomerization and caspase-1 activation.
Accordingly, Annexin a2-deficient mice were more susceptible to A.
phagocytophilum infection and showed splenomegaly, thrombocytopenia, and
monocytopenia. Providing translational support to our findings, better binding of
annexin A2 to sialostatin L2 in sera from 21 out of 23 infected patients than in
sera from control individuals was also demonstrated. Overall, we establish a
unique mode of inflammasome evasion by a pathogen, centered on a blood-feeding
arthropod.
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