Antiviral mechanism study of sulfated polysaccharidesf
- VernacularTitle:Сульфатжсан полисахаридын вирүсийн эсрэг үйлдлийн механизмын судалгаа
- Author:
Tungalag Battulga
1
;
Takashi Yoshida
2
Author Information
1. School of Pharmacy, MNUMS
2. Kitami Institute of Technology, Japan
- Publication Type:Journal Article
- Keywords:
human immunodeficiency virus;
influenza virus;
oligopeptide;
interaction
- From:Mongolian Medical Sciences
2021;196(2):3-7
- CountryMongolia
- Language:Mongolian
-
Abstract:
Background:Sulfated polysaccharides have specific antiviral activities, which biological mechanism is assumed to
the electrostatic interaction between (+)-charged virus surface glycoproteins and (-)-charged sulfate
groups.
Objective:For the elucidation of the mechanism, several oligopeptides referenced by the sequence of Human
Immunodeficiency Virus glycoprotein 120 (HIV gp120) and hemagglutinin (HA) of influenza A and
B were synthesized by a peptide synthesizer and the interaction with structurally distinct sulfated
polysaccharides such as curdlan sulfate and dextran sulfate was analyzed by SPR.
Method:In this study, six oligopeptides were synthesized from the sequence of the V3 loop, C-terminus, and
CD4 binding domain in the HIV gp120. Oligopeptide A from the V3 loop comprises 20 amino acids with
seven positively charged lysine and arginine in the sequence. The basic amino acids were relatively
dispersed along the sequence compared with that of oligopeptide B. Likewise, oligopeptide B from
the C–terminus comprises seven lysine and arginine, also oligopeptide of Influenza A/Yamagata
HA and Influenza A/Brisbane HA comprises 23 amino acids with eight positively charged lysine and
arginine in the sequence. Oligopeptide C from the CD4 binding domain and Influenza B /Hong Kong
from the HA comprises one lysine and next to the biotin. The biotinylated peptides were synthesized
by a microwave assisted solid phase peptide synthesizer using Fmoc protected amino acids. The
peptides were purified by RP-HPLC and identified the structure by using MALDI TOF MS.
Result:Peptides A and B from HIV gp120 were found to have interacted strongly with dextran and curdlan
sulfates, however, the peptide C without positively charged amino acids showed no interaction.
These results suggest that the interaction was due to the electrostatic interaction between negatively
charged sulfate groups and positively charged amino groups of the peptides. The results of influenza
HAs, influenza A (Yamagata and Brisbane) and B (Hong Kong) viruses, are also presented.
Conclusion:Curdlan and dextran sulfates were found to increase the interaction with increasing the molecular
weights and degree of sulfation (DS), which were found to be important factors for the antiviral activity
of sulfated polysaccharides. Based on the above, suggesting the antivirus mechanism of sulfated
polysaccharides to be the electrostatic interaction of negatively charged sulfated polysaccharides
and virus surface glycoprotein at the positively charged amino acid regions.
- Full text:2021-196(2)-3-7.pdf
