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2017 ; 12
(10
): e0186780
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CLEC9A modulates macrophage-mediated neutrophil recruitment in response to
heat-killed Mycobacterium tuberculosis H37Ra
#MMPMID29065139
Cheng AC
; Yang KY
; Chen NJ
; Hsu TL
; Jou R
; Hsieh SL
; Tseng PH
PLoS One
2017[]; 12
(10
): e0186780
PMID29065139
show ga
Tuberculosis is a fatal human infectious disease caused by Mycobacterium
tuberculosis (M. tuberculosis) that is prevalent worldwide. Mycobacteria differ
from other bacteria in that they have a cell wall composed of specific surface
glycans that are the major determinant of these organisms' pathogenicity. The
interaction of M. tuberculosis with pattern recognition receptors (PRRs), in
particular C-type lectin receptors (CLRs), on the surface of macrophages plays a
central role in initiating innate and adaptive immunity, but the picture as a
whole remains a puzzle. Defining novel mechanisms by which host receptors
interact with pathogens in order to modulate a specific immune response is an
area of intense research. In this study, based on an in vitro lectin binding
assay, CLEC9A (DNGR-1) is identified as a novel CLR that binds with mycobacteria.
Our results with CLEC9A-knocked down cells and a CLEC9A-Fc fusion protein as
blocking agents show that CLEC9A is involved in the activation of SYK and MAPK
signaling in response to heat-killed M. tuberculosis H37Ra treatment, and it then
promotes the production of CXCL8 and IL-1? in macrophages. The CXCL8 and IL-1?
secreted by the activated macrophages are critical to neutrophil recruitment and
activation. In a in vivo mouse model, when the interaction between CLEC9A and
H37Ra is interfered with by treatment with CLEC9A-Fc fusion protein, this reduces
lung inflammation and cell infiltration. These findings demonstrate that CLEC9A
is a specialized receptor that modulates the innate immune response when there is
a mycobacterial infection.
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