Serine protease autotransporters of
Enterobacteriaceae
(SPATEs) are secreted proteins that contribute to virulence and function as proteases, toxins, adhesins, and/or immunomodulators. An extra-intestinal pathogenic
E. coli
(ExPEC) O1:K1 strain, QT598, isolated from a turkey, was shown to contain
vat, tsh
, and three uncharacterized SPATE-encoding genes. Uncharacterized SPATEs: Sha (
S
erine-protease
h
emagglutinin
a
utotransporter), TagB and TagC (
t
andem
a
utotransporter
g
enes
B
and
C
) were tested for activities including hemagglutination, autoaggregation, and cytotoxicity when expressed in
E. coli
K-12. Sha and TagB conferred autoaggregation and hemagglutination activities. TagB, TagC, and Sha all exhibited cytopathic effects on a bladder epithelial cell line. In QT598,
tagB
and
tagC
are tandemly encoded on a genomic island, and were present in 10% of UTI isolates and 4.7% of avian
E. coli
. Sha is encoded on a virulence plasmid and was present in 1% of UTI isolates and 20% of avian
E. coli
. To specifically examine the role of SPATEs for infection, the 5 SPATE genes were deleted from strain QT598 and tested for cytotoxicity. Loss of all five SPATEs abrogated the cytopathic effect on bladder epithelial cells, although derivatives producing any of the 5 SPATEs retained cytopathic activity. In mouse infections,
sha
gene-expression was up-regulated a mean of sixfold in the bladder compared to growth
in vitro
. Loss of either
tagBC
or
sha
did not reduce urinary tract colonization. Deletion of all 5 SPATEs, however, significantly reduced competitive colonization of the kidney supporting a cumulative role of SPATEs for QT598 in the mouse UTI model.