The ability of enteropathogenic salmonellae to recruit inflammatory cells a
nd induce secretory responses in the infected ileum is considered to be a m
ain feature in Salmonella-induced enteritis, Interactions between the patho
gen and intestinal epithelial cells result in a variety of cellular respons
es mediating inflammation and fluid secretion. It is becoming apparent that
proteins secreted by the Inv-Spa type III secretion system of Salmonella s
pp. play a key role in the induction of these responses. We have recently d
emonstrated that the SopB effector protein is translocated into eukaryotic
cells via a Sip-dependent pathway and mediates inflammation and fluid secre
tion in infected ileal mucosa. However, SopB did not appear to be the only
effector involved, as inactivation of the sopB gene only partially impaired
enteropathogenicity. We suggested that at least some of such protein effec
ters are likely to be proteins of the same class as SopB, i.e., secreted ef
fector proteins translocated into eukaroyotic cells via a Sip dependent pat
hway. In this work, we identify SopD, another secreted protein belonging to
the family of Sop effecters of Salmonella dublin. Using the cya reporter s
ystem,ve showed that SopD is translocated into eukaroyotic cells, We assess
ed the potential involvement of SopD in enteropathogenicity and found that
inactivation of sopD has an additive effect in relation to the sopB mutatio
n.