Inhibition of respiratory syncytial virus by RhoA-derived peptides: implications for the development of improved antiviral agents targeting heparin-binding viruses

被引：16

作者：

Budge, PJ

Graham, BS

机构：

[1] NIAID, Viral Pathogenesis Lab, Vaccine Res Ctr, NIH, Bethesda, MD 20892 USA

[2] Vanderbilt Univ, Med Ctr, Dept Microbiol & Immunol, Nashville, TN 37232 USA

来源：

JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY | 2004年 / 54卷 / 02期

关键词：

RSV; polyanions; fusion inhibition; dextran sulphate; sulphated polysaccharides; antiviral agents; post-attachment neutralization; human immunodeficiency virus; HIV; heparin; heparan sulphate;

D O I：

10.1093/jac/dkh355

中图分类号：

R51 [传染病];

学科分类号：

100401 ;

摘要：

The respiratory syncytial virus (RSV) fusion glycoprotein (F) can interact with the small intracellular GTPase RhoA, and peptides derived from RhoA inhibit RSV replication. These observations initially suggested that RhoA-derived peptides might inhibit RSV replication by disrupting an in vivo interaction between RSV F and RhoA. However, recent data indicate that the antiviral activity of RhoA-derived peptides is not due to competitive inhibition of an hypothesized F-RhoA interaction, but is rather a function of the peptides' intrinsic biophysical properties. We summarize here what is known about the mechanism of RSV inhibition by these peptides and give our opinion regarding the potential implications of this work with regards to RSV biology, and to the development of antiviral agents targeting RSV and other enveloped viruses.

引用

页码：299 / 302

页数：4

共 37 条

[1]

BATINIC D, 1992, J BIOL CHEM, V267, P6664

[2] RhoA-derived peptide dimers share mechanistic properties with other polyanionic inhibitors of respiratory syncytial virus (RSV), including disruption of viral attachment and dependence on RSV G [J].