Genes,
Journal Year:
2024,
Volume and Issue:
15(11), P. 1476 - 1476
Published: Nov. 15, 2024
(TRIM26)
is
an
E3
ubiquitin
ligase
and
a
member
of
the
TRIM
family.
Similar
to
other
proteins,
TRIM26
consists
three
domains,
collectively
termed
RBCC:
Really
Interesting
New
Gene
(RING)
domain,
one
B-Box
C
terminal
domain
consisting
PRY/SPRY
domain.
The
exhibits
relatively
higher
conservation
compared
with
RING
suggesting
potentially
similar
roles
across
proteins
from
various
species.
either
directly
interacts
viral
or
modulates
immune
responses
engage
infection,
serving
as
protective
detrimental
host
factor
depending
on
circumvent
infection.
present
review
focuses
understanding
mechanisms
during
infection
its
potential
future
applications.
Viruses,
Journal Year:
2025,
Volume and Issue:
17(5), P. 644 - 644
Published: April 29, 2025
Flaviviruses
are
usually
transmitted
to
humans
via
mosquito
or
tick
bites,
whose
infections
may
lead
severe
diseases
and
fatality.
During
intracellular
infection,
they
remodel
the
endoplasmic
reticulum
(ER)
membrane
generate
compartments
scaffolding
replication
complex
(RC)
where
of
viral
genome
takes
place.
In
this
study,
we
purified
ER
fraction
virus
infected
cells
identify
proteins
that
were
enriched
during
flavivirus
infection.
We
found
tripartite
motif-containing
(TRIMs)
including
TRIM38,
TRIM21,
TRIM14
significantly
infection
with
mosquito-borne
(West
Nile
strain
Kunjin
Zika
(ZIKV))
tick-borne
(Langat
(LGTV))
flaviviruses.
Further
characterizations
showed
TRIM21
act
as
restriction
factors
against
ZIKV
LGTV,
while
TRIM38
hinders
These
TRIMs
worked
interferon-stimulated
genes
mediate
IFN-I
response
LGTV
infections.
Restriction
by
coincides
their
colocalization
NS3.
TRIM14-mediated
its
NS3
NS5
proteins.
However,
did
not
colocalize
protein
suggesting
antiviral
activity
is
dependent
on
direct
targeting
enzyme.
Finally,
demonstrated
overexpression
restricted
replication.
Frontiers in Immunology,
Journal Year:
2024,
Volume and Issue:
15
Published: June 12, 2024
TRIM21
is
a
pivotal
effector
in
the
immune
system,
orchestrating
antibody-mediated
responses
and
modulating
signaling.
In
this
comprehensive
study,
we
focus
on
interaction
of
with
Fc
engineered
antibodies
subsequent
implications
for
viral
neutralization.
Through
series
analytical
techniques,
including
biosensor
assays,
mass
photometry,
electron
microscopy,
along
structure
predictions,
unravel
intricate
mechanisms
governing
interplay
between
antibodies.
Our
investigations
reveal
that
capacity
to
recognize,
bind,
facilitate
proteasomal
degradation
antibody-coated
viruses
critically
dependent
affinity
avidity
its
interactions
antibody
regions.
We
suggest
novel
binding
mechanism,
where
one
site
results
detachment
PRYSPRY
from
coiled-coil
domain,
enhancing
mobility
due
flexible
linker,
thereby
facilitating
engagement
second
site,
resulting
bivalent
engagement.
These
findings
shed
light
dual
role
antiviral
immunity,
both
recognizing
directing
intracellular
degradation,
demonstrate
potential
therapeutic
exploitation.
The
study
advances
our
understanding
opens
new
avenues
development
strategies
innovation
tailored
functions
designed
leverage
TRIM21s
unique
mode.
Life Science Alliance,
Journal Year:
2024,
Volume and Issue:
7(9), P. e202402786 - e202402786
Published: July 8, 2024
The
ubiquitin-like
modifier
FAT10
is
upregulated
under
pro-inflammatory
conditions,
targets
its
substrates
for
proteasomal
degradation
and
functions
as
a
negative
regulator
of
the
type-I
IFN
response.
Influenza
A
virus
infection
upregulates
production
expression
E3
ligase
TRIM21,
which
regulates
in
positive
feedback
manner.
In
this
study,
we
show
that
becomes
covalently
conjugated
to
TRIM21
degradation.
We
further
coiled-coil
PRYSPRY
domains
C-terminal
diglycine
motif
are
important
TRIM21-FAT10
interaction.
Moreover,
upon
influenza
presence
total
ubiquitination
reduced
our
data
reveal
FAT10-mediated
diminishes
IFNβ
production.
Overall,
study
provides
strong
evidence
down-regulates
antiviral
by
modulating
additional
molecules
RIG-I
signaling
pathway
besides
already
published
OTUB1.
addition,
elucidate
novel
mechanism
stability.
Microbial Cell Factories,
Journal Year:
2023,
Volume and Issue:
22(1)
Published: Dec. 18, 2023
RNA-dependent
RNA
polymerase
(RdRp)
is
a
good
target
of
anti-RNA
virus
agents;
not
only
it
pivotal
for
the
replication
cycle
and
highly
conserved
among
viruses
across
different
families,
but
also
lacks
human
homolog.
Recently,
single-chain
antibody
(HuscFv)
that
bound
to
thumb
domain
hepatitis
C
(HCV)
(functionalized
NS5B
protein)
was
produced
engineered
into
cell-penetrating
(super
antibody)
in
form
peptide
(penetratin,
PEN)-linked
HuscFv
(PEN-HuscFv34).
The
super
purified
from
inclusion
body
(IB)
pen-huscfv34-vector-transformed
Escherichia
coli.
inhibited
alpha-
beta-
coronaviruses,
flaviviruses,
picornaviruses
were
tested
(broadly
effective);
thus,
has
high
potential
developing
further
towards
pan-anti-RNA
agent.
However,
production,
purification,
refolding
molecules
bacterial
IB
are
laborious
hurdles
large-scale
production.
Therefore,
this
study,
Sortase-self-cleave
method
bacteria
surface
display
system
combined
modified
production.BL21
(DE3)
ΔA
E.
coli,
strain
lacking
predominant
outer
membrane
protein
(OmpA)
ion
OmpT
proteases,
displayed
membrane-anchored
fusion
protein,
i.e.,
chimeric
lipoprotein
(Lpp')-OmpA',
SUMO,
Sortase
protease,
cleavage
site
(LPET↓G)
PEN-HuscFv34-6×
His
generated.
soluble
with
glycine
at
N-terminus
could
be
released
coli
surface,
simply
by
incubating
cells
Sortase-cleavage
buffer.
After
centrifugation,
G-PEN-HuscFv34-6×
supernatant.
retained
original
ability
(being
broadly
effective
activity
IB-derived-PEN-HuscFv34.The
functionalized
RdRp
successfully
using
self-cleave
systems
modification.
suitable
downstream
processing
production
antibody.
It
applicable
other
recombinant
proteins
free-folding
form.
Genes,
Journal Year:
2024,
Volume and Issue:
15(11), P. 1476 - 1476
Published: Nov. 15, 2024
(TRIM26)
is
an
E3
ubiquitin
ligase
and
a
member
of
the
TRIM
family.
Similar
to
other
proteins,
TRIM26
consists
three
domains,
collectively
termed
RBCC:
Really
Interesting
New
Gene
(RING)
domain,
one
B-Box
C
terminal
domain
consisting
PRY/SPRY
domain.
The
exhibits
relatively
higher
conservation
compared
with
RING
suggesting
potentially
similar
roles
across
proteins
from
various
species.
either
directly
interacts
viral
or
modulates
immune
responses
engage
infection,
serving
as
protective
detrimental
host
factor
depending
on
circumvent
infection.
present
review
focuses
understanding
mechanisms
during
infection
its
potential
future
applications.