3.2.1.18: exo-alpha-sialidase
This is an abbreviated version!
For detailed information about exo-alpha-sialidase, go to the full flat file.
Word Map on EC 3.2.1.18
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3.2.1.18
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influenza
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sialic
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viruses
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vaccine
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pandemic
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oseltamivir
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lectin
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sialylated
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oligosaccharide
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subtype
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epitope
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erythrocyte
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gangliosides
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lymphocyte
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reassortant
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hemagglutination
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anti-influenza
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chicken
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glycans
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surveillance
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galactose
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cholera
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desialylation
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hn
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glycoconjugates
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outbreak
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cruzi
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poultry
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virion
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bird
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pronase
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parainfluenza
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epidemic
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n-acetylneuraminic
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trypanosoma
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peanut
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mucin
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n-linked
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newcastle
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agglutination
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perfringens
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nucleoprotein
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prophylaxis
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concanavalin
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medicine
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drift
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sendai
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analysis
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n-acetylgalactosamine
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ferret
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nutrition
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endoglycosidase
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molecular biology
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diagnostics
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gm3
- 3.2.1.18
- influenza
-
sialic
- viruses
- vaccine
- pandemic
- oseltamivir
- lectin
-
sialylated
- oligosaccharide
- subtype
- epitope
- erythrocyte
- gangliosides
- lymphocyte
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reassortant
-
hemagglutination
-
anti-influenza
- chicken
- glycans
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surveillance
- galactose
- cholera
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desialylation
- hn
- glycoconjugates
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outbreak
- cruzi
-
poultry
- virion
- bird
- pronase
- parainfluenza
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epidemic
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n-acetylneuraminic
- trypanosoma
- peanut
- mucin
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n-linked
- newcastle
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agglutination
- perfringens
- nucleoprotein
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prophylaxis
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concanavalin
- medicine
-
drift
-
sendai
- analysis
- n-acetylgalactosamine
- ferret
- nutrition
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endoglycosidase
- molecular biology
- diagnostics
- gm3
Reaction
Synonyms
acetylneuraminidase, Acetylneuraminyl hydrolase, acid sialidase, acylneuraminyl glycohydrolase, alpha-N-acylneuraminate glycohydrolase, alpha-neuraminidase, alpha-sialidase, alpha2,6-sialidase, alpha2,6-sialyltransferase, alpha2,6-trans-sialidase, Am0705, Am0707, Am1757, Am2085, Cytosolic sialidase, DELTA15Pd2,6ST, endo-N, endo-N-acylneuraminidase, endo-sialidase, endoNF, endosialidase, exo-alpha-sialidase, exo-sialidase, G9 sialidase, Ganglioside sialidase, ganglioside-specific sialidase, GH33C, glycosyl hydrolase, haemagglutinin-neuraminidase protein, hemagglutinin-neuraminidase, hemagglutinin-neuraminidase glycoprotein, HN, HsNEU2, IID sialidase, KDNase, Lysosomal sialidase, Major 85 kDa surface antigen, Major surface antigen, Membrane sialidase, MmNEU3, More, Mouse skeletal muscle sialidase, MSS, MTS, mucopolysaccharide N-acetylneuraminylhydrolase, Murine thymic sialidase, N-acetyl-alpha-neuraminidase, N-acetyl-alpha-neuraminidase 1, N-acetyl-alpha-neuraminidase 2, N-acetyl-alpha-neuraminidase 3, N-acetyl-alpha-neuraminidase 4, N-acetylneuraminosyl glycohydrolase, N-acylneuraminate glycohydrolase, N-acylneuraminosyl glycohydrolase, NA, NA1, NA2, NAN1, NanA, NANase, NanB, NanC, NanH, NanI, NanICD, NanJ, NanPs, Neu, NEU1, NEU2, Neu3, Neu3a, Neu3d, Neu3e, NEU4, NEU4 long, NEU4 short, NEU4L, Neu4L sialidase, neuramindase, neuraminidase, neuraminidase 1, neuraminidase 2, neuraminidase 3, neuraminidase-1, PA2794, SA85-1.1 protein, SA85-1.2 protein, SA85-1.3 protein, SiaBb1, sialidase, sialidase 4, sialidase II, sialidase Neu2, sialidase-2, sialidase-3, sialidase-4, sialidase/neuraminidase mutant F129A, sialyl hydrolase, STNA, TcTS, TDE0471, Tr6, trans-sialidase, trans-sialidase 1, TSia, VCNA
ECTree
3.2.1.18 exo-alpha-sialidaseAdvanced search results
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results (Engineering
Engineering on EC 3.2.1.18 - exo-alpha-sialidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D84A
the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
R171L
the mutant has higher activity on a N-acetylneuraminic acid-based substrate than wild type enzyme
Y358H
the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
D84A
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the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
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R171L
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the mutant has higher activity on a N-acetylneuraminic acid-based substrate than wild type enzyme
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Y358H
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the mutation significantly lowers the activity of the enzyme, but this mutant remains a retaining glycosidase
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E258D
site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
E347K
A2THD4, A7L4X3, A7UC53, A7UC55, A7UC57, A7UC61, A7UC62, A7UC63, A7UC64, A7UC67, A7UC69, A7UC70, Q83758, Q914X2, Q9W8Z8
the mutation affects the reactivity of polyclonal serum to the variant strain
I192M
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naturally occuring mutant with a single nucleotide mutation T-A at position 576, isolation of a NDV variant with highly increased fusogenic activity in vitro and decreased haemagglutinating activity, as compared with the wild-type parental strain, phenotype of the virus in cell cultures, embryonated chicken eggs and day-old chickens, overview
R498K
site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
R498Q
site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
S418A
site-directed mutagenesis, mutation of a catalytic residue, unaltered sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
Y262F
site-directed mutagenesis, mutation of a catalytic residue, retaining of nearly all sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
Y262S
site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
Y317A
site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
Y317F
site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
Y317S
site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
I192M
Avian orthoavulavirus 1 Anhinga/US(FL)/44083/93
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naturally occuring mutant with a single nucleotide mutation T-A at position 576, isolation of a NDV variant with highly increased fusogenic activity in vitro and decreased haemagglutinating activity, as compared with the wild-type parental strain, phenotype of the virus in cell cultures, embryonated chicken eggs and day-old chickens, overview
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E347K
Avian orthoavulavirus 1 Herts/33
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the mutation affects the reactivity of polyclonal serum to the variant strain
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R498K
Avian orthoavulavirus 1 Kansas
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site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
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R498Q
Avian orthoavulavirus 1 Kansas
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site-directed mutagenesis, mutation of a catalytic residue, highly reduced sialidase activity, slightly reduced HA activity, mutant shows reduced fusion promotion activity
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S418A
Avian orthoavulavirus 1 Kansas
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site-directed mutagenesis, mutation of a catalytic residue, unaltered sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
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Y317A
Avian orthoavulavirus 1 Kansas
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site-directed mutagenesis, mutation of a catalytic residue, loss of nearly all sialidase activity, highly reduced HA activity, mutant shows reduced fusion promotion activity
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Y317F
Avian orthoavulavirus 1 Kansas
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site-directed mutagenesis, mutation of a catalytic residue, reduced sialidase activity, altered HA activity, mutant shows reduced fusion promotion activity
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E347K
Avian orthoavulavirus 1 ZJ-01/00
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the mutation affects the reactivity of polyclonal serum to the variant strain
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R294K
A160G
site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme
D234N
the mutation results in significantly lower levels of sialidase activity (25%) compared to the wild type and is associated with sialosis
D50S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E51D
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E51S
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
G162A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G413A
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site-directed mutagenesis, activity and localization in the cell similar to the wild-type enzyme
G419STOP
site-directed mutagenesis, the C-terminal 10-residue truncation leads to an increase in activity compared to the wild-type enzyme
H277F
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I105G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K45A
the mutant shows about 3fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
L408STOP
site-directed mutagenesis, the large deletion leads to inactivation of the mutant
L415A
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site-directed mutagenesis, 30-50% reduced activity compared to the wild-type enzyme, no internalization due to impaired endocytosis, location in the plasma membrane and the cytosol
M87G
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N88D
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q112A
the mutant shows nearly 4fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
Q270A
the mutant shows about 4fold increased activity towards 4-methylumbelliferyl-alpha-D-N-acetylneuraminic acid compared to the wild type
R114A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R114Q
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R25H
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
V107M
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
V217A
the mutation results in significantly lower levels of sialidase activity (44%) compared to the wild type and is associated with sialosis
Y370C
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y370F
Y412A
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site-directed mutagenesis, 55-70% reduced activity compared to the wild-type enzyme, no internalization due to impaired endocytosis, location in the plasma membrane and the cytosol
N173S
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mutant sensitive to 4-azido-5-isobutyrylamino-2,3-didehydro-2,3,4,5-tetradeoxy-d-glycero-d-galacto-2-nonulopyranosic acid in neuraminidase inhibition assays but more than 10000fold less sensitive to the compound in hemagglutination inhibition tests than a recombinant Sendai virus whose hemagglutinin-neuraminidase is replaced with that of human parainfluenza virus-1. Its susceptibility to 4-azido-5-isobutyrylamino-2,3-didehydro-2,3,4,5-tetradeoxy-d-glycero-d-galacto-2-nonulopyranosic acid in plaque reduction assays is reduced fivefold and does not differ from that of recombinant Sendai virus whose hemagglutinin-neuraminidase was replaced with that of human parainfluenza virus-1 in mice. The N173S mutant fails to be efficiently eluted from erythrocytes and released from cells. It demonstrates reduced growth in cell culture and superior growth in mice. Rresults are consistent with the loss of the N-linked glycan at residue 173 in the mutant. Study suggests that the N-linked glycan at residue 173 masks a second receptor-binding site
D198N
D198N/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119A/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119D
E119D/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E119G/H274Y
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
E245G
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neuraminidase activity is 73% of wild-type value. IC50 for zanamivir is 2.9fold higher than wild-type value. IC50 for oseltamivir is 2.3fold higher than wild-type value
H274Y
I222L
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neuraminidase activity is 82% of wild-type value. IC50 for zanamivir is 5.1fold higher than wild-type value. IC50 for oseltamivir is 18fold higher than wild-type value
N146K/A272V/Del245-248
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revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N146K/S219T/A272V
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revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N146K/S219T/A272V/Del245-248
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mutant isolated from an oseltamivir-resistant virus from an immunocompromised child. The deletion is the sole change responsible for resistance
N146K/S219T/Del245-248
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revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
N294D
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neuraminidase activity is 74% of wild-type value. IC50 for zanamivir is 2.4fold higher than wild-type value. IC50 for oseltamivir is 2.3fold higher than wild-type value
N294S
the mutation confers reduced inhibition to oseltamivir (63.6fold increase in IC50 compared to the wild type)
Q136K
the neuraminidase mutation has no effect on oseltamivir susceptibility but causes approximately a 300fold and a 70fold reduction in zanamivir and peramivir susceptibility, respectively. The mutant strain displays greater viral fitness than the wild-type virus in MDCK cells but equivalent infectivity and transmissibility in a ferret model
R152K
the mutant exhibits reduced inhibition to oseltamivir (17.9fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
R292K
the mutant exhibits reduced inhibition to oseltamivir (33fold in IC50 values) but shows wild type inhibition to zanamivir and peramivir
S219T/A272V/Del245-248
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revertant constructed from mutant N146K/S219T/A272V/Del245-248 for analysis of resistance to oseltamivir
H274Y
-
the mutation confers resistance to oseltamivir, the viral fitness of the A/Brisbane/59/2007-like H274Y variant is not impaired
D199E
-
the mutant shows increased enzyme activity compared to the wild type enzyme
E119D
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the mutation confers reduced inhibition by oseltamivir (a 95-fold increase in the 50% inhibitory concentration) and highly reduced inhibition by zanamivir, peramivir. and laninamivir (2660fold, 460fold, and 651fold increases in the 50% inhibitory concentration, respectively)
E119G
-
the mutation confers mainly reduced to highly reduced inhibition by zanamivir, peramivir, and laninamivir, but remains susceptible to oseltamivir
H275Y
the major oseltamivir resistance mutation H275Y causes a significant decrease in the enzyme's ability to bind oseltamivir
H275Y/I223V
the mutations result in extreme impairment of oseltamivir's inhibition potency
H275Y/S247N
the mutations result in extreme impairment of oseltamivir's inhibition potency
I223V
the substitution alone confers only a moderate reduction in oseltamivir affinity
I321V
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
K432E
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N200S
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N248D
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N270K
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the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N369K
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
N386K
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
P458T
-
the mutant with decreased activity exhibits highly reduced inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
Q136K
-
the mutation confers mainly reduced to highly reduced inhibition by zanamivir, peramivir, and laninamivir, but remains susceptible to oseltamivir
R152K
-
the mutant remains susceptible to peramivir, but confers reduced inhibition by zanamivir, oseltamivir, and laninamivir
S247N
the substitution alone confers only a moderate reduction in oseltamivir affinity
V264I
-
the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
E119D
influenza A virus H1N1 pdm09
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the mutation confers reduced inhibition by oseltamivir (a 95-fold increase in the 50% inhibitory concentration) and highly reduced inhibition by zanamivir, peramivir. and laninamivir (2660fold, 460fold, and 651fold increases in the 50% inhibitory concentration, respectively)
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N200S
influenza A virus H1N1 pdm09
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the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
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N248D
influenza A virus H1N1 pdm09
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the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
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N386K
influenza A virus H1N1 pdm09
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the mutant shows normal inhibition by zanamivir, peramivir, laninamivir and oseltamivir compared to the wild type enzyme
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R152K
influenza A virus H1N1 pdm09
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the mutant remains susceptible to peramivir, but confers reduced inhibition by zanamivir, oseltamivir, and laninamivir
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S389R
the mutation decreases enzymatic activity for transferrin and increases enzymatic activity for fetuin
G140R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
P139S
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the mutation is associated with reduced susceptibility to neuraminidase inhibitors
Q138R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
R152K
the mutation leads to resistance against nfluenza virus neuraminidase inhibitors
G140R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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P139S
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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Q138R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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G140R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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P139S
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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Q138R
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the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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G140R
-
the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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P139S
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the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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Q138R
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the mutation is associated with reduced susceptibility to neuraminidase inhibitors
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Y370A
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 4% of the activity with Y370G
Y370G
Y370N
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370N
Y370T
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration, 9% of the activity with Y370T
E335K
D59A
H274Y
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 265, for inhibition by zanamivir is 1.9, respectively
N294S
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mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 81, for inhibition by zanamivir is 7.2, respectively
R152K
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
R152K/V94I
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the mutations mediate reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
R368K
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir and laninamivir (96-57fold increase of IC50 value compared to the wild type enzyme) as well as peramivir (172fold increase of IC50 value compared to the wild type enzyme)
V94IK
-
the mutant shows normal inhibition by oseltamivir, zanamivir, peramivir and laninamivir
Y252H
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 0.1, for inhibition by zanamivir is 1.2, respectively
R152K
unidentified influenza virus A/Quebec/144147/09
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
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R152K/V94I
unidentified influenza virus A/Quebec/144147/09
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the mutations mediate reduced inhibition by oseltamivir, zanamivir, peramivir and laninamivir (10-100fold increase of IC50 value compared to the wild type enzyme)
-
R368K
unidentified influenza virus A/Quebec/144147/09
-
the mutation mediates reduced inhibition by oseltamivir, zanamivir and laninamivir (96-57fold increase of IC50 value compared to the wild type enzyme) as well as peramivir (172fold increase of IC50 value compared to the wild type enzyme)
-
V94IK
unidentified influenza virus A/Quebec/144147/09
-
the mutant shows normal inhibition by oseltamivir, zanamivir, peramivir and laninamivir
-
H274Y
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 265, for inhibition by zanamivir is 1.9, respectively
-
N294S
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 81, for inhibition by zanamivir is 7.2, respectively
-
Y252H
-
mutant isolated from patient infected with H5N1. Ratio Ki mutant/Ki wild-type for inhibition by oseltamivir is 0.1, for inhibition by zanamivir is 1.2, respectively
-
additional information
R294K
the substitution confers neuraminidase inhibitor oseltamivir resistance, The mutation results in reduced enzyme catalytic efficiency along with lower viral fitness
R294K
H7N9 subtype A/Anhui/1/2013
-
the substitution confers neuraminidase inhibitor oseltamivir resistance, The mutation results in reduced enzyme catalytic efficiency along with lower viral fitness
-
R294K
H7N9 subtype A/Shanghai/1/2013
-
the substitution confers neuraminidase inhibitor oseltamivir resistance, The mutation results in reduced enzyme catalytic efficiency along with lower viral fitness
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D198N
-
neuraminidase activity is 10% of wild-type value. IC50 for zanamivir is 5fold higher than wild-type value. IC50 for oseltamivir is 5.5fold higher than wild-type value
D198N
the mutation moderately affects the susceptibility to neuraminidase inhibitors
E119D
the mutation confers reduced inhibition to zanamivir, oseltamivir, and peramivir
H274Y
-
neuraminidase activity is 104% of wild-type value. IC50 for zanamivir is 3.2fold higher than wild-type value. IC50 for oseltamivir is 9.4fold higher than wild-type value
H274Y
-
mutant resistant to oseltamivir, used for design of multi-binding-site inhibitors
H274Y
the mutation confers highly reduced inhibition to oseltamivir (1131.4fold increase in IC50 values compared to the wild type) and reduced inhibition to peramivir by 50.6fold
Y370G
catalyzes the hydrolysis of phenyl beta-sialoside with an inversion of the anomeric configuration
Y370G
the mutation produces an efficient catalyst for the transfer of N-acetylneuraminic acid from an artificial substrate (i.e., phenyl N-acetyl-beta-D-neuraminide) to a sugar acceptor (e.g., D-lactose, D-glucose, D-mannose, D-raffinose, D-allose, or D-fructose) to give N-acetyl-alpha-neuraminide coupled carbohydrate products. In addition, this mutant enzyme catalyzes the transfer of a sugar residue from the artificial substrate 2-fluorophenyl N-acetyl-beta-D-neuraminide to methyl glycopyranoside acceptors
E335K
-
the mutation is associated with neurovirulence of Urabe AM9 mumps virus vaccine
E335K
Mumps orthorubulavirus Urabe AM9
-
the mutation is associated with neurovirulence of Urabe AM9 mumps virus vaccine
-
D59A
-
catalytic acid/base residue mutation, crystal structure determination, altered catalytic mechanism and enzyme-substrate structure compared to the wild-type enzyme, respectively
D59A
-
replacement of putative acid/base catalyst, demonstration of the half-reaction with formation of sialyl-enzyme intermediate. Activity is restored by addition of azide and a sialyl azide product is formed
additional information
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a mutant strain, with cysteine residue of the active site being exchanged for other amino acids, is insensitive to inhibition by mercury ions
additional information
purified truncated NanH protein devoid of its signal sequence as a mature enzyme fused with the 6-His tag at the N-terminal region can cleave alpha-2,3- and alpah-2,6-linked sialic acid from sialic acid-containing substrates and is able to catalyse the transfer of sialic acid using several sialoconjugates as donor
additional information
-
purified truncated NanH protein devoid of its signal sequence as a mature enzyme fused with the 6-His tag at the N-terminal region can cleave alpha-2,3- and alpah-2,6-linked sialic acid from sialic acid-containing substrates and is able to catalyse the transfer of sialic acid using several sialoconjugates as donor
additional information
-
purified truncated NanH protein devoid of its signal sequence as a mature enzyme fused with the 6-His tag at the N-terminal region can cleave alpha-2,3- and alpah-2,6-linked sialic acid from sialic acid-containing substrates and is able to catalyse the transfer of sialic acid using several sialoconjugates as donor
-
additional information
mutations of residues expected to interact directly with the sialic acid N5-acetyl (A160, M87, I105) and C7-C9 glycerol side-chain (E113, Y179, Y181) reduce enzymatic activity. Truncations at the N- or C-terminus of more than 10 residues abolish enzyme activity
additional information
-
mutations of residues expected to interact directly with the sialic acid N5-acetyl (A160, M87, I105) and C7-C9 glycerol side-chain (E113, Y179, Y181) reduce enzymatic activity. Truncations at the N- or C-terminus of more than 10 residues abolish enzyme activity
additional information
-
construction of a soluble truncation mutant, amino acid residues 137-575, lacking the N-terminal hydrophobic membrane anchoring region, mutant shows increased sensitivity to inhibition by DANA
additional information
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study on the effects of single-point amino acid substitutions on the structure and function of neuraminidase proteins. The rate of tolerant random one amino acid substitutions is 47%. Rates of tolerant substitutions for the stalk and for the surface and inner portion are 79%, 54%, and 19%, respectively. The ratio of mutations with which the enzyme loses neuraminidase activity, but is transported to the cell surface, decreases in proportion to the distance from the structural center of enzyme active site
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construction of insertion mutant enzyme by deleting the 20-aa segment, residues 49-68, from the stalk region of 2009H1N1 neuraminidase, and inserting this segment, designated 09s60, into the stalk region of H5N1 neuraminidase
additional information
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construction of insertion mutant enzyme by deleting the 20-aa segment, residues 49-68, from the stalk region of 2009H1N1 neuraminidase, and inserting this segment, designated 09s60, into the stalk region of H5N1 neuraminidase
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additional information
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construction of insertion mutant enzyme by deleting the 20-aa segment, residues 49-68, from the stalk region of 2009H1N1 neuraminidase, and inserting this segment, designated 09s60, into the stalk region of H5N1 neuraminidase
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additional information
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study on the effects of single-point amino acid substitutions on the structure and function of neuraminidase proteins. The rate of tolerant random one amino acid substitutions is 47%. Rates of tolerant substitutions for the stalk and for the surface and inner portion are 79%, 54%, and 19%, respectively. The ratio of mutations with which the enzyme loses neuraminidase activity, but is transported to the cell surface, decreases in proportion to the distance from the structural center of enzyme active site
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replacement of the F protein of parainfluenza virus 5 major domains, M1, M2, M3, and M4, and five minor domains, A to E, in the middle region of the PIV5 F protein with the simian virus 41, SV41, F counterparts individually or in combination. A chimera designated M(1+2), which harbored SV41 F-derived domains M1 and M2, mediates cell-cell fusion with the coexpressed SV41 hemagglutinin-neuraminidase protein, suggesting that these domains are involved in determining the hemagglutinin-neuraminidase protein specificity. Another chimera which harbors the SV41 F-derived domain B in addition to domains M1 and M2 shows increased specificity for the SV41 hemagglutinin-neuraminidase protein compared to that of M(1+2), although it is capable of mediating cell-cell fusion by itself
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amino acids R180, D204, E264, Y268, Y303, E407, R422, R512, Y540, E551 constitute the neuraminidase active site and directly interact with sialic acid
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Mumps orthorubulavirus Urabe AM9
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amino acids R180, D204, E264, Y268, Y303, E407, R422, R512, Y540, E551 constitute the neuraminidase active site and directly interact with sialic acid
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in macrophages from isoform Neu1 deficient mice, a model for sialidosis, oversialylated lysosomal membrane protein Lamp-1 enhances lysosomal exocytosis. Silencing of Lamp-1 reverts this phenotype by interfering with the docking of lysosomes at the plasma membrane. In Neu1-/- mice the excessive exocytosis of serine proteases in the bone niche leads to inactivation of extracellular serpins, premature degradation of VCAM-1, and loss of bone marrow retention
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neuramindase-1 deficiency in mice results in a tight-skin phenotype. Normal septation of Neu-1 null mice does not occur in neonatal mice, resulting in enlarged alveoli that are maintained in adults. Elastin fibers develop abnormally and elastin, fibrillin-1, fibrillin-2, and fibrillin-5 show overlapping distributions. Myofibroblasts distribute randomly around the alveolar walls. Concentration of elastin is significantly reduced in the aorta of mutant mice
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insertional inactivation of nanH results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
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insertional inactivation of nanH results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
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insertional inactivation of nanH results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
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insertional inactivation of nanH, encoding the second sialidase of the organism, results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
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insertional inactivation of nanH, encoding the second sialidase of the organism, results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
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insertional inactivation of nanH, encoding the second sialidase of the organism, results in a mutant, which is not deficient in sialidase production, but exhibits reduced activity
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in neuraminidase NanA deletion mutant, NanB can partially support the growth of pneumococci on glycoconjugates
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in neuraminidase NanA deletion mutant, NanB can partially support the growth of pneumococci on glycoconjugates
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subcloning of a 56500 Da domain that retains full enzymatic activity
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subcloning of a 56500 Da domain that retains full enzymatic activity
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introduction of 7 surface mutations does not alter the enzymes' activities but facilitate crystallization
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engineering of an enzymatically deficient mutant trans-sialidase containing the catalytic domain without the immunodominant shed acute phase antigen repeats SAPA. Mice vaccinated with the mutant trans-sialidase are highly protected against Trypanosoma cruzi infection
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construction of highly infectious laryngotracheitis virus expressing H5 hemagglutinin and N1 neuraminidase for ocular immunization of chickens
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fusion of gene encoding the neuraminidase N1 head domain residues 63-449 with the Saccharomyces cerevisiae alpha-factor secretion signal and expression in Pichia pastoris. Recombinant product is a soluble protein with similar kinetic characteristics as wild-type
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construction of highly infectious laryngotracheitis virus expressing H5 hemagglutinin and N1 neuraminidase for ocular immunization of chickens
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subcloning of carbohydrate-binding module CBM40 of sialidase, showing high affinity for sialic acid and specificity to alpha(2,3), alpha(2,6), and alpha(2,8)-linked sialosides. Creation of polypeptides containing up to four CBM40 modules in tandem show increased affinities compared with the single module molecule. Variation in linker length has little effect on affinity
