Direct inactivation of herpes simplex virus type-2 by rat epidermal protein.
Proteins were extracted from corneocytes of skin of 2-day-old rats and fractionated by gel filtration and cation exchange column chromatography. The different protein fractions were tested for direct inactivation of herpes simplex virus infectivity as determined by reduction of plaque formation. The most effective protein fractions against herpes simplex virus were a neutral pH buffer soluble and mol. wts. ranging from 20 K to 30 K. Amino acid composition of the proteins were virtually identical to epidermal histidine-rich proteins. The activity was significantly (P less than 0.001) stronger against type-2 than type-1. The activity was most stable at pH 7.2 and the rate of inhibition increased in a time-dependent manner up to 4 h. The 50% effective dose was estimated as 1.1 micrograms protein/ml.
Shimozuma
M
M
Department of Dermatology, University of California, San Francisco 94143-0536.
Drew
W L
WL
Miner
R C
RC
Epstein
W L
WL
Fukuyama
K
K
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D000998:Antiviral Agents / Q000502:physiology*; D002852:Chromatography, Ion Exchange; D004817:Epidermis / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D011506:Proteins / Q000737:chemistry / Q000494:pharmacology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D018139:Simplexvirus / Q000187:drug effects*; D010948:Viral Plaque Assay
D000596:Amino Acids; D000998:Antiviral Agents; D011506:Proteins