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Cytotoxic glucosyltransferases of Legionella pneumophila.
[legionellosis]
Legionella
is
a
gram-negative
bacterium
and
the
causative
pathogen
of
legionellosis
-a
severe
pneumonia
in
humans
.
A
large
number
of
Legionella
effectors
interfere
with
numerous
host
cell
functions
,
including
intracellular
vacuole
trafficking
and
maturation
,
phospholipid
metabolism
,
protein
ubiquitination
,
pro-
/
anti-apoptotic
balances
or
inflammatory
responses
.
Moreover
,
eukaryotic
protein
synthesis
is
affected
by
L
.
pneumophila
glucosyltransferases
Lgt
1
,
Lgt
2
,
and
Lgt
3
.
Structurally
,
these
enzymes
are
similar
to
large
clostridial
cytotoxins
,
use
UDP-glucose
as
a
co
-substrate
and
modify
a
conserved
serine
residue
(
Ser-
53
)
in
elongation
factor
1
A
(
eEF
1
A
)
.
The
ternary
complex
consisting
of
eEF
1
A
,
GTP
,
and
aminoacylated-t
RNA
seems
to
be
the
substrate
for
Lgts
.
Studies
with
Saccharomyces
cerevisiae
corroborated
that
eEF
1
A
is
the
major
target
responsible
for
Lgt-induced
cytotoxic
activity
.
In
addition
to
Lgt
proteins
,
Legionella
produces
other
effector
glycosyltransferase
,
including
the
modularly
composed
protein
SetA
,
which
displays
tropism
for
early
endosomal
compartments
,
subverts
host
cell
vesicle
trafficking
and
demonstrates
toxic
activities
toward
yeast
and
mammalian
cells
.
Here
,
our
current
knowledge
about
both
groups
of
L
.
pneumophila
glycosylating
effectors
is
reviewed
.
Diseases
Validation
Diseases presenting
"severe pneumonia in humans"
symptom
legionellosis
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