Amino acid substitutions in glycoprotein D mediate the ability of fusion from without-positive herpes simplex virus type 1 strains to penetrate at 4 degrees and in the presence of soluble glycoprotein D.
In former studies, we described herpes simplex virus type 1 (HSV-1) strains ANG, ANG path and HSZP as strains with special fusion activities, caused by mutations in the syn 3 locus. In this report, we describe the special penetration properties of these strains: their ability to penetrate at 4 degrees and to overcome the infection block caused by soluble glycoprotein D-1 (gD-1) in the medium. Using intertypic recombinants of HSV-1 strains ANG path and KOS, we showed that these penetration properties are the result of two mutations in amino acids 25 (Leu-Pro) and 27 (Gln-Arg) in the N-terminal part of the mature gD-1 glycoprotein.
Lingen
M
M
Institut für Virologie, Johannes-Gutenberg Universität, Mainz, Germany.
Seck
T
T
Dehoust
U
U
Weise
K
K
Falke
D
D
D000596:Amino Acids / Q000502:physiology; D000818:Animals; D001665:Binding Sites; D002522:Chlorocebus aethiops; D006224:Cricetinae; D003412:Cricetulus; D005260:Female; D008561:Membrane Fusion; D009154:Mutation; D011993:Recombinant Fusion Proteins; D015183:Restriction Mapping; D018139:Simplexvirus / Q000235:genetics / Q000502:physiology*; D013696:Temperature; D014709:Vero Cells; D010948:Viral Plaque Assay; D014764:Viral Proteins / Q000235:genetics / Q000502:physiology*
D000596:Amino Acids; D011993:Recombinant Fusion Proteins; D014764:Viral Proteins; C046998:bovine herpesvirus type-1 glycoproteins