Excretion of Non-infectious Virus Particles Lacking Glycoprotein H by a Temperature-sensitive Mutant of Herpes Simplex Virus Type 1: Evidence that gH Is Essential for Virion Infectivity

Abstract

SUMMARYA temperature-sensitive mutant of herpes simplex virus type 1, tsQ26, was shown to contain an amino acid substitution in glycoprotein H (gH). The mutant entered cells efficiently at the non-permissive temperature and replicated to give nearly normal yields of intracellular infectivity. The intracellular virions contained, predominantly, an immature form ofgH and no gH was found on the surface of infected cells. Excreted virions were devoid of gH and were not infectious. Virions excreted at the permissive temperature were infectious and contained gH and no loss of gH resulted from incubation of these virions at the non-permissive temperature. The temperaturesensitive phenotype apparently results from the loss of gH from virions during their transport to the cell surface, and since loss of gH is accompanied by loss of infectivity we conclude that gH is an essential component of the infectious virion.

HSV trafficking and development of gene therapy vectors with applications in the nervous system

“…gB, gD, gH, and gL are essential for viral infection, [31][32][33][34] while gC, gE, gG, gI, gJ, gK, and gM are dispensable for infection in vitro. [2][3][4] Some glycoproteins form functional homo-oligomers (eg gB), [35][36][37][38][39][40] while others form functional hetero-oligomers (gH/gL, gI/ gE).…”

Induction of protective immunity with antibody to herpes simplex virus type 1 glycoprotein H (gH) and analysis of the immune response to gH expressed in recombinant vaccinia virus

“…Glycoprotein H (gH) of herpes simplex virus type 1 (HSV-1) is one of three glycoproteins that are essential for virus viability in tissue culture (Cai et al, 1988 ;Ligas & Johnson, 1988;Desai et al, 1988), and homologues of this glycoprotein have been identified in members of all the herpesvirus subfamilies (Davison & Taylor, 1987;Gompels et al, 1988;Cranage et al, 1988;Heineman et al, 1988). gH is required for virus entry (Desai et al, 1988) and is probably involved in cell to cell spread of infectivity since gH-specific monoclonal antibodies (MAbs), in addition to neutralizing free virus, inhibit cell fusion by syncytial strains and prevent intercellular virus transmission (Buckmaster et al, 1984;Gompels & Minson, 1986).…”

“…gH is required for virus entry (Desai et al, 1988) and is probably involved in cell to cell spread of infectivity since gH-specific monoclonal antibodies (MAbs), in addition to neutralizing free virus, inhibit cell fusion by syncytial strains and prevent intercellular virus transmission (Buckmaster et al, 1984;Gompels & Minson, 1986). Antibodies raised against the varicellazoster virus and Epstein-Barr virus homologues have similar properties implying functional conservation (Keller et al, 1987;Miller & Hutt-Fletcher, 1988).…”

“…Ascites fluids used for passive immunizations contained 3 to 5 mg/ml IgG. AntitrpE-gH is a rabbit serum raised against a tryptophan E-HSV-1 gH fusion protein (Desai et al, 1988). Neutralization assays were performed as described by Minson et al (1986).…”

Specific targeted binding of herpes simplex virus type 1 to hepatocytes via the human hepatitis B virus preS1 peptide

“…Moreover, the virus envelope contains at least 11 glycoproteins (gB, gC, gD, gE, gG, gH, gI, gJ, gK, gL, and gM) among which only gB, gD, gH, and gL are essential for viral infection in cell culture, but the others can be required for some specific functions or infection of particular cell surfaces in vivo. [46][47][48][49][50] Depending on the need, the manipulation of both essential and accessory glycoproteins may prove useful for construction of HSV targeted vectors.…”