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) st rains 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 s oluble glycoprotein D-1 (gD-1) in the medium. Using intertypic recombi nants of HSV-1 strains ANG path and KOS, we showed that these penetrat ion 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 glycop rotein.