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Cited by 195

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Isolation of an Antiviral Polysaccharide, Nostoflan, from a Terrestrial Cyanobacterium, Nostoc flagelliforme

Kanekiyo, Kenji, Lee, Jung-Bum, Hayashi, Kyoko, Takenaka, Hiroyuki, Hayakawa, Yumiko, Endo, Shunro, Hayashi, Toshimitsu·2005·Journal of Natural Products

Abstract

A novel acidic polysaccharide, nostoflan, was isolated from a terrestrial cyanobacterium, Nostoc flagelliforme. Nostoflan exhibited a potent anti-herpes simplex virus type 1 (HSV-1) activity with a selectivity index (50% cytotoxic concentration/50% inhibitory concentration against viral replication) of 13,000. Sugar composition and methylation analyses revealed that it was mainly composed of -->4)-D-Glcp-(1-->, -->6,4)-D-Glcp-(1-->, -->4)-D-Galp-(1-->, -->4)-D-Xylp-(1-->, D-GlcAp-(1-->, D-Manp-(1--> with a ratio of ca. 1:1:1:1:0.8:0.2. Two pyridylaminated oligosaccharides were prepared by partial acid hydrolysis and pyridylamination. On the basis of MALDI-TOF-MS and NMR analyses, they were found to be beta-D-Glcp-(1-->4)-D-Xyl-PA and beta-D-GlcAp-(1-->6)-beta-D-Glcp-(1-->4)-D-Gal-PA. From these results, nostoflan might be mainly composed of the following two types of sugar sequence: -->4)-beta-D-Glcp-(1-->4)-D-Xylp-(1--> and -->4)-[beta-D-GlcAp-(1-->6)-]-beta-D-Glcp-(1-->4)-D-Galp-(1-->. Besides anti-HSV-1 activity, nostoflan showed potent antiviral activities against HSV-2, human cytomegalovirus, and influenza A virus, but no activity against adenovirus and coxsackie virus was observed. Therefore, nostoflan has a broad antiviral spectrum against enveloped viruses whose cellular receptors are carbohydrates. Furthermore, nostoflan showed no antithrombin activity, unlike sulfated polysaccharides.

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Metadata

Authors
Kanekiyo, K., Lee, J.-B., Hayashi, K., Takenaka, H., Hayakawa, Y., Endo, S., & Hayashi, T.
Venue
Journal of Natural Products
Published
2005-06-11
Volume
68
Issue
7
Pages
1037-1041
ISSN
  • 0163-3864 (ISSN-L)
  • 1520-6025
OpenAlex
W2033526052
Cited by
195
References
2
FWCI
8.57
Type
journal article
Language
en
Open access
closed

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