The virucidal EB peptide protects host cells from herpes simplex virus type 1 infection in the presence of serum albumin and aggregates proteins in a detergent-like manner.

Antimicrobial Agents and Chemotherapy
Hermann BultmannCurtis R Brandt

Abstract

The linear cationic amphiphilic EB peptide, derived from the FGF4 signal sequence, was previously shown to be virucidal and to block herpes simplex type I (HSV-1) entry (H. Bultmann, J. S. Busse, and C. R. Brandt, J. Virol. 75:2634-2645, 2001). Here we show that cells treated with EB (RRKKAAVALLPAVLLALLAP) for less than 5 min are also protected from infection with HSV-1. Though protection was lost over a period of 5 to 8 h, it was reinduced as rapidly as during the initial treatment. Below a 20 μM concentration of EB, cells gained protection in a serum-dependent manner, requiring bovine serum albumin (BSA) as a cofactor. Above 40 μM, EB coprecipitated with BSA under hypotonic conditions. Coprecipitates retained antiviral activity and released active peptide. NaCl (≥0.3 M) blocked coprecipitation without interfering with antiviral activity. As shown for β-galactosidase, EB below 20 μM acted as an enzyme inhibitor, whereas above 40 to 100 μM EB, β-galactosidase was precipitated as was BSA or other unrelated proteins. Pyrene fluorescence spectroscopy revealed that in the course of protein aggregation, EB acted like a cationic surfactant and self associated in a process resembling micelle formation. Both antiviral activity and prot...Continue Reading

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Citations

Jan 12, 2011·Antimicrobial Agents and Chemotherapy·Jeremy C JonesStacey Schultz-Cherry
Jan 10, 2012·Virology Journal·Sharon E AltmannJoseph E Blaney
May 2, 2014·Biochimica Et Biophysica Acta·Hussain BadaniWilliam C Wimley
Jan 15, 2013·ChemMedChem·Peter Michael Moyle, Istvan Toth
Nov 6, 2018·Frontiers in Microbiology·Francisco J IbáñezPablo A González
Oct 30, 2019·Microorganisms·Raghuram KogantiDeepak Shukla
Jun 1, 2021·Frontiers in Plant Science·Karen Lizbeth Reyes-BarreraÁngel Gabriel Alpuche-Solís

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