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General Information
DRAVP ID DRAVPe02190
Peptide Name Alstotide As1
Sequence CRPYGYRCDGVINQCCDPYHCTPPLIGICL
Sequence Length 30
UniProt ID A0A0S0ZR07
Taxon ID 52822
Source Alstonia scholaris plant
Validation Experimentally Validated
Origin Information
Gene Name/ID As1
GenBank Not Available
Amino Acid position 63-92
Domain Accession ID Not Available
Nucleotide sequence ID Not Available
Molecular Type Not Available
Chromosomal Position Not Available
Activity Information
Target Organism IBV
Assay Antiviral Activity Assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target S protein
Mechanism We first determined the stage(s) in viral replication cycle which alstotides could inhibit using a time of drug addition assay. As1 (50 and 100 μm) was introduced to synchronized infected cells at different time points during preincubation at 4 °C and the infection at 37 °C As1 was identified as a moderate early acting anti-IBV drug, as supported by three lines of evidence. First, the time of drug addition assay revealed a significant drop of activity when As1 was added at 3 hpi, implicating an antiviral mechanism upstream of genomic replication and gene expression. Second, in transfection assay when the genetic material was electroporated into the host cells to bypass the attachment and entry steps, no inhibition over gene replication within 18 hpi was observed. In contrast, parallel As1-treated samples collected at 40 hpi showed a clear inhibition, probably because of inhibitory activity during the early stage of secondary infection. Third, As1 binds to IBV fusion glycoprotein, S protein, which plays a vital role during viral entry by attaching to Vero cell receptors and triggering membrane fusion between enveloped virus and host cells. In this assay, As1 added during attachment (at 4 °C) or entry (after transfer to 37 °C) exhibited comparable positive effects. As1 significantly lost its activity when added during later stages from 3 hpi onward. Comparable intensities of the endogenous control actin bands for both the treated and untreated samples excluded the effect of As1 on cellular protein synthesis, thus suggesting that As1 acts during an early stage of the viral infection.
Structure Information
PDB ID 2MM6
Predicted Structure Download No predicted structure available
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C145H222N40O41S6
Absent amino acids AEKMFWOU
Common amino acids C
Mass 3373.96
Pl 6.7
Basic residues 2
Acidic residues 2
Hydrophobic residues 24
Net charge 0
Boman Index 0.9576
Hydrophobicity 0.063
Aliphatic Index 74.67
Half Life
Extinction Coefficient cystines 4470
Absorbance 280nm 1.35
Polar residues 32
Literature Information
Literature 1
Title Antiviral Cystine Knot α-Amylase Inhibitors from Alstonia scholaris
Pubmed ID 26546678
Reference The Journal of biological chemistry, 290(52), 31138–31150.
Author Nguyen, P. Q., Ooi, J. S., Nguyen, N. T., Wang, S., Huang, M., Liu, D. X., & Tam, J. P. (2015).
To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.