Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2014 Apr 7:14:131.
doi: 10.1186/1472-6882-14-131.

Prophylactic effect of herbal-marine compound (HESA-A) on influenza A virus infectivity

Affiliations

Prophylactic effect of herbal-marine compound (HESA-A) on influenza A virus infectivity

Parvaneh Mehrbod et al. BMC Complement Altern Med. .

Abstract

Background: Influenza virus is still a severe respiratory disease affecting human and other species. As conventional drugs are not recommended for long time because of side effects and drug resistance occurrence, traditional medication has been focused as alternative remedy. HESA-A is a natural compound from herbal-marine origin. Previous studies have reported the therapeutic properties of HESA-A on psoriasis vulgaris and different types of cancers and we also showed its anti-inflammatory effects against influenza A infection.

Methods: This study was designed to investigate the potential properties of HESA-A as prophylaxis or treatment. To investigate the prophylaxis or treatment activities of HESA-A, Madin-Darby Canine Kidney (MDCK) cells were exposed to HESA-A and influenza A virus in different manners of exposure and different time intervals. The results were evaluated by MTT and HA assays.

Results: It was found that HESA-A is much more effective against influenza cytopathic effects when it is applied for prophylaxis and also in concurrent treatment (p ≤ 0.05) but not in post-infection treatment (p ≥ 0.05).

Conclusion: In conclusion, HESA-A is significantly effective against influenza replication in prophylaxis application affecting the virus penetration/adsorption to the cell without any toxic effect on the cell viability.

PubMed Disclaimer

Figures

Figure 1
Figure 1
Cell viability in combination treatments. Data shows the MTT assay results for cell viability of HESA-A treatments against influenza A virus H1N1 CPE in different exposure types and time points. Data are presented as mean ± SD. *: Significantly different from values obtained for co- & pre-treatments as compared to the virus sample (p < 0.05).
Figure 2
Figure 2
Log HA titer reduction in HESA-A treatments against H1N1. The HA data showed highly significant decrements in all combination treatments as compared to the H1N1 sample. Data are presented as mean ± SD. **: Highly significantly different from values obtained for combination treatments as compared to the virus sample (p < 0.01).

Similar articles

Cited by

References

    1. Sarah CD, Hong M. Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel. Proc Natl Acad Sci USA. 2008;105:1483–1488. doi: 10.1073/pnas.0711500105. - DOI - PMC - PubMed
    1. Calero M, Chen CZ, Zhu W, Winand N, Havas KA, Gilbert PM, Burd CG, Collins RN. Dual prenylation is required for Rab protein localization and function. Mol Biol Cell. 2003;14:1852–1867. doi: 10.1091/mbc.E02-11-0707. - DOI - PMC - PubMed
    1. Wagman PC, Leong MA, Simmen KA. Development of a novel influenza A antiviral assay. J Virol Method. 2002;105:105–114. doi: 10.1016/S0166-0934(02)00088-5. - DOI - PubMed
    1. Dai J-P, Li W-Z, Zhao X-F, Wang G-F, Yang J-C, Zhang L, Chen X-X, Xu Y-X, Li K-S. A drug screening method based on the autophagy pathway and studies of the mechanism of evodiamine against influenza A virus. PLoS One. 2012;7:e42706. doi: 10.1371/journal.pone.0042706. - DOI - PMC - PubMed
    1. Pathumwadee I, Chittima L, Thanyada R, Arthorn L, Maturos M, Panita D, Ornjira A, Krit C, Nopphorn K, Pornthep S, Somsak P, Supot H. How amantadine and rimantadine inhibit proton transport in the M2 protein channel. J Mol Graph Model. 2008;27:342–348. doi: 10.1016/j.jmgm.2008.06.002. - DOI - PubMed

Publication types