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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Biochem+J
2012 ; 445
(3
): 383-92
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Recruitment and membrane interactions of host cell proteins during attachment of
enteropathogenic and enterohaemorrhagic Escherichia coli
#MMPMID22587461
Munera D
; Martinez E
; Varyukhina S
; Mahajan A
; Ayala-Sanmartin J
; Frankel G
Biochem J
2012[Aug]; 445
(3
): 383-92
PMID22587461
show ga
EPEC (enteropathogenic Escherichia coli) and EHEC (enterohaemorrhagic Escherichia
coli) are attaching and effacing pathogens frequently associated with infectious
diarrhoea. EPEC and EHEC use a T3SS (type III secretion system) to translocate
effectors that subvert different cellular processes to sustain colonization and
multiplication. The eukaryotic proteins NHERF2 (Na(+)/H(+) exchanger regulatory
factor 2) and AnxA2 (annexin A2), which are involved in regulation of intestinal
ion channels, are recruited to the bacterial attachment sites. Using a stable
HeLa-NHERF2 cell line, we found partial co-localization of AnxA2 and NHERF2; in
EPEC-infected cells, AnxA2 and NHERF2 were extensively recruited to the site of
bacterial attachment. We confirmed that NHERF2 dimerizes and found that NHERF2
interacts with AnxA2. Moreover, we found that AnxA2 also binds both the N- and
C-terminal domains of the bacterial effector Tir through its C-terminal domain.
Immunofluorescence of HeLa cells infected with EPEC showed that AnxA2 is
recruited to the site of bacterial attachment in a Tir-dependent manner, but
independently of Tir-induced actin polymerization. Our results suggest that AnxA2
and NHERF2 form a scaffold complex that links adjacent Tir molecules at the
plasma membrane forming a lattice that could be involved in retention and
dissemination of other effectors at the bacterial attachment site.