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Information on EC 3.4.21.91 - Flavivirin and Organism(s) Yellow fever virus and UniProt Accession P03314
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3.4.21.91 FlavivirinSpecify your search results
Word Map
- 3.4.21.91
- polyprotein
- viruses
- ns4a
-
replicons
-
west
- ribavirin
-
anti-hcv
-
direct-acting
-
virologic
-
cirrhosis
-
flaviviral
- boceprevir
- flaviviruses
- encephalitis
-
pegylated
- flaviviridae
- telaprevir
-
subgenomic
-
rna-dependent
-
unwind
-
mosquito-borne
- asunaprevir
-
resistance-associated
-
daclatasvir
- simeprevir
-
hcv-infected
- coronaviruses
-
anti-dengue
- ntpase
-
peptidomimetic
-
nonnucleoside
-
hcv-specific
-
macrodomains
- drug development
-
treatment-naive
-
peginterferon
-
replicase
-
quasispecies
-
interferon-free
-
trans-cleavage
- alphavirus
-
positive-stranded
- sofosbuvir
- analysis
- molecular biology
-
rna-stimulated
- medicine
-
hcv-1b
- synthesis
- gt1
The taxonomic range for the selected organisms is: Yellow fever virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Selective hydrolysis of -Xaa-Xaa-/-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala
Synonyms
ns3 protease, nonstructural protein 3, ns2b-ns3 protease, ns3 serine protease, ns2b-ns3pro, ns2b/ns3 protease, ns3 proteinase, ns3pro, ns2b/ns3, zikv protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
NS2B-3 proteinase
-
-
-
-
Yellow fever virus (flavivirus) protease
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
154215-26-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Bz-Nle-Lys-Arg-Arg-7-amido-4-methylcoumarin + H2O
?
-
10fold higher affinity for the tetrapeptide than for the tripeptide Boc-Gly-Arg-Arg-7-amido-4-methylcoumarin, and processes it with 34fold greater efficiency
-
-
?
N-alpha-benzoyl-L-arginine-p-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + p-nitroaniline
-
-
-
-
?
NS2B-3181-polyproteins + H2O
?
-
effect of mutations within Gly-Ala-Arg-Arg-+-Ser sequence on cis-cleavage (mutations at P1', P1, P2, P3 and P4), the term-+- depicts the point of cleavage
-
-
?
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGKR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRK + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AGRR + SAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-AKRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARKR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRK + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-ARRR + SQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KKR + SSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine + H2O
o-aminobenzoyl-KRR + SSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide + H2O
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine + 7-amino-4-methylcoumarin
-
-
-
-
?
YF17D virus protein + H2O
?
-
cleavage site: Gln-Gln-Arg-+-Ser, i.e. 4A/2K site, this cleavage is prerequisite for processing at the downstream signalase site, determinants of cleavage site specificity for 2B/3 cleavage (site: Gly-Ala-Arg-Arg-+-Ser), the term-+- depicts the point of cleavage
-
-
?
Yellow fever virus protein + H2O
?
-
cleavage sites: 2A/2B, 2B/3, 3/4A and 4B/5, 4 dibasic sites in nonstructural region of viral polyprotein
-
-
?
additional information
?
-
-
viral serine protease consisting of viral protein NS2B and NS3
-
-
?
additional information
?
-
-
amino-terminal third of NS3 acts as serine protease on nonstructural viral proteins
-
-
?
additional information
?
-
-
cleavage preference for substrates containing basic amino acids
-
?
additional information
?
-
-
the recombinant NS2B-NS3 protease is subject to autolytic cleavage
-
-
?
additional information
?
-
-
docking studies of the bioactive compounds at the active site of NS2B-NS3 complex also indicate 4-hydroxypanduratin A as potential lead compound for drug development
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NS2B cofactor
N-terminal region of NS3 and its cofactor NS2B constitute the protease. To function as an active enzyme, the NS3 protease requires the NS2B cofactor. NS2B is an integral membrane protein of 14 kDa that contains three domains: two trans-membrane segments located at the N- and C-termini and a central region of 47 amino acids (spanning amino-acids 49-96) that acts as an essential protein cofactor of the NS3 protease
-
NS2B protein
-
all cleavages of the flavivirus polyprotein mediated by the NS3 protease are believed to require cofactor activity of the NS2B protein
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
-
kcat/Km values decrease by adding NaCl up to 100 mM. This results from the systematic increase in Km values with the increase in NaCl concentration in the range 1 to 10 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
inhibitor potency is driven predominantely by interactions with amino acid residues in the S1 and S2 pockets, as substitutions in the P1 and P2 sites have the greates impact on inhibitor potency. P1 and P2 positions are most important for inhibitor binding, whilst the P3 and P4 positions have much less effect
-
additional information
-
N-alpha-benzoyl-L-arginine-p-nitroanilide causes precipitation of the recombinant protease and is therefore not appropiate for enzymatic analysis
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0087
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0073
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.005
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.02
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0066
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0076
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0006
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.002
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.00013
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.014
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0015
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0096
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.012
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.0021
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.415
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.53
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.01
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.005
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.061
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.004
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.097
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.012
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.026
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.002
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.06
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.005
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.12
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.012
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.025
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.044
t-butyloxycarbonyl-glycyl-L-arginyl-L-arginine-4-methylcoumaryl-7-amide
-
-
0.006
t-butyloxycarbonyl-glycyl-L-lysyl-L-arginine-4-methylcoumaryl-7-amide
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
o-aminobenzoyl-AGKKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
1.37
o-aminobenzoyl-AGKRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
1
o-aminobenzoyl-AGRKSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
3.04
o-aminobenzoyl-AGRRSAQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
0.6
o-aminobenzoyl-AKKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
12.8
o-aminobenzoyl-AKKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
20
o-aminobenzoyl-AKRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
13
o-aminobenzoyl-AKRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
18.16
o-aminobenzoyl-ARKKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
4.08
o-aminobenzoyl-ARKRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
3.33
o-aminobenzoyl-ARRKSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
12.5
o-aminobenzoyl-ARRRSQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
1
o-aminobenzoyl-KKRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
11.9
o-aminobenzoyl-KRRSSKQ-N-(2,4-dinitrophenyl)-ethylenediamine
-
pH 9.0, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10.5
7 - 10.5
-
at pH 9.0 the enzyme is 5times more active than at pH 7.0, and more than 3times more active than at pH 10.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
the flavivirus NS3 protein is associated with the endoplasmic reticulum membrane via its close interaction with the central hydrophilic region of the NS2B integral membrane protein
-
additional information
-
cytoplasmic localization with membrane association
-
additional information
-
NS2B is membrane component of viral replication process, presumably responsible for membrane localization of NS3
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
the N-terminal region of NS3 and its cofactor NS2B constitute the protease that cleaves the viral polyprotein. The NS3 C-terminal domain possesses RNA helicase, nucleoside and RNA triphosphatase activities and is involved both in viral RNA replication and virus particle formation. NS2B-NS3 protein plays multiple roles in the virus life cycle. NS2B-NS3 serves as a hub for the assembly of the flavivirus replication complex and also modulates viral pathogenesis and the host immune response
additional information
enzyme ligand binding structure analysis, three-dimensional enzyme structure analysis
PDB
SCOP
CATH
UNIPROT
ORGANISM
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
mutation studies at the residues His94, Asp118 and Ser176 reveal that Asp118-His94 bond play an important role in the structural stability of NS2B-NS3 complex
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
deltaNS2B-NS3pro and deltaNS2B-NS3proHDA expressed as a hexahistidine-tagged protein in Escherichia coli BL21-CodonPlus(DE3)-RIL cells
-
plasmid pYFV-NS2B40-G4SG4-HM-NS3FL expressed in Escherichia coli strain Rosetta2
-
single-chain complex of NS2B/NS3 protease (CF40-gly-NS3pro190) expressed as an N-terminally His-tagged fusion protein in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
flavivirus NS2B-NS3 protease-helicase is a target for antiviral drug development
drug development
-
characteristics of Yellow fever virus protease are very similar to those reported for dengue and West Nile virus proteases, and suggest that pan-flavivirus NS3 protease drugs may be developed for flaviviral diseases
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chambers, T.J.; Hahn, C.S.; Galler, R.; Rice, C.M.
Flavivirus genome organization, expression, and replication
Annu. Rev. Microbiol.
44
649-688
1990
Dengue virus, Flavivirus sp., Yellow fever virus
Lin, C.; Amberg, S.M.; Chambers, T.J.; Rice, C.M.
Cleavage at a novel site in the NS4A region by the yellow fever virus NS2B-3 proteinase is a prerequisite for processing at the downstream 4A/4B signalase site
J. Virol.
67
2327-2335
1993
Yellow fever virus
Chambers, T.J.; Nestorowicz, A.; Rice, C.M.
Mutagenesis of the yellow fever virus NS2B/3 cleavage site: determinants of cleavage site specificity and effects on polyprotein processing and viral replication
J. Virol.
69
1600-1605
1995
Yellow fever virus
Droll, D.A.; Krishna Murthy, H.M.; Chambers, T.J.
Yellow fever virus NS2B-NS3 protease: charged-to-alanine mutagenesis and deletion analysis define regions important for protease complex formation and function
Virology
275
335-347
2000
Yellow fever virus
Bera, A.K.; Kuhn, R.J.; Smith, J.L.
Functional characterization of cis and trans activity of the Flavivirus NS2B-NS3 protease
J. Biol. Chem.
282
12883-12892
2007
Japanese encephalitis virus, West Nile virus, Yellow fever virus, Dengue virus type 2, Dengue virus type 4, West Nile virus NY99
Loehr, K.; Knox, J.E.; Phong, W.Y.; Ma, N.L.; Yin, Z.; Sampath, A.; Patel, S.J.; Wang, W.L.; Chan, W.L.; Rao, K.R.; Wang, G.; Vasudevan, S.G.; Keller, T.H.; Lim, S.P.
Yellow fever virus NS3 protease: peptide-inhibition studies
J. Gen. Virol.
88
2223-2227
2007
Yellow fever virus
Bessaud, M.; Pastorino, B.A.; Peyrefitte, C.N.; Rolland, D.; Grandadam, M.; Tolou, H.J.
Functional characterization of the NS2B/NS3 protease complex from seven viruses belonging to different groups inside the genus Flavivirus
Virus Res.
120
79-90
2006
Yellow fever virus, Zika virus, Saint Louis encephalitis virus, Bussuquara virus, Langat virus (P29837), Dengue virus type 3 (Q6YMS4), dengue virus type I (Q91NH1), Yellow fever virus Asibi, Dengue virus type 3 Sri Lanka/1266/2000 (Q6YMS4), dengue virus type I D1/H/IMTSSA/98/606 (Q91NH1), Langat virus TP21 (P29837), Zika virus Ar-D-41644, Saint Louis encephalitis virus MSI-7
Kondo, M.Y.; Oliveira, L.C.; Okamoto, D.N.; de Araujo, M.R.; Duarte dos Santos, C.N.; Juliano, M.A.; Juliano, L.; Gouvea, I.E.
Yellow fever virus NS2B/NS3 protease: hydrolytic properties and substrate specificity
Biochem. Biophys. Res. Commun.
407
640-644
2011
Yellow fever virus
Kannappan, P.; Narayanan, S.
Mutation and docking studies on NS2b-NS3 complex from yellow fever virus towards drug discovery
Bioinformation
6
303-306
2011
Yellow fever virus
Luo, D.; Vasudevan, S.G.; Lescar, J.
The flavivirus NS2B-NS3 protease-helicase as a target for antiviral drug development
Antiviral Res.
118
148-158
2015
Yellow fever virus (P03314), Murray Valley encephalitis virus (P05769), West Nile virus (P06935), Kunjin virus (P14335), dengue virus type I (P17763), Japanese encephalitis virus (P27395), Dengue virus type 2 (P29990), Dengue virus type 4 (Q2YHF0), Kokobera virus (Q32ZD5), Dengue virus type 3 (Q6YMS3), Dengue virus type 2 Thailand/16681/1984 (P29990), Dengue virus type 3 Martinique/1243/1999 (Q6YMS3), Yellow fever virus 17D vaccine (P03314), Dengue virus type 4 Thailand/0348/1991 (Q2YHF0), dengue virus type I Nauru/West Pac/1974 (P17763), Japanese encephalitis virus SA-14 (P27395), Kunjin virus MRM61C (P14335), Murray Valley encephalitis virus MVE-1-51 (P05769)
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