Nucleotide sequence of a herpes simplex virus type 1 gene that causes cell fusion

DebRoy, Chitrita; Pederson, Nels E.; Person, Stanley

doi:10.1016/0042-6822(85)90199-0

Cited by 119 publications

(140 citation statements)

References 52 publications

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“…Mutations of this type occur in the gB coding sequence (Manservigi et al, 1977;Honess et al, 1980;Bzik et al, 1984) and in a recently sequenced open reading frame at map position 0.74 on the HSV-1 physical map (Bond & Person, 1984;Debroy et al, 1985). It is notable that those antibodies which suppressed the syncytial phenotype were also the most effective in inhibiting the enlargement of plaques (i.e.…”

Section: Discussionmentioning

confidence: 99%

An Analysis of the Biological Properties of Monoclonal Antibodies against Glycoprotein D of Herpes Simplex Virus and Identification of Amino Acid Substitutions that Confer Resistance to Neutralization

Minson

Hodgman

Digard

et al. 1986

Journal of General Virology

179

183

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SUMMARYFour monoclonal antibodies to glycoprotein D (gD) of herpes simplex virus (HSV) types 1 and 2 neutralized virus in the presence of complement but exhibited diverse activities in its absence. Amino acid substitutions that conferred resistance to neutralization by each antibody were identified by deriving the nucleotide sequence of the gD gene from resistant mutants. Each antibody selected a substitution from different parts of the molecule and mutants resistant to a single antibody always arose from the same mutation. One of the antibodies reacted with a synthetic oligopeptide corresponding to the region of the molecule in which amino acid substitution conferred resistance, but the remaining three antibodies failed to react with predicted oligopeptide targets. These antibodies may therefore react with 'discontinuous' epitopes, a view supported by the observation that two of these three antibodies competed with each other in binding assays despite the fact that substitutions conferring resistance to neutralization arose nearly 100 residues apart in the primary sequence. The four antibodies had very different biological properties. One antibody neutralized infectivity but did not inhibit cell fusion, one antibody inhibited cell fusion but did not neutralize, while a third antibody had both activities. One antibody had neither activity but enhanced the infectivity of HSV-2 in a type-specific manner. The ability of antibodies to inhibit cell fusion by syncytial virus strains correlated with an ability to prevent plaque enlargement by a non-syncytial virus strain, implying a role for gD in the intercellular spread of virus that is independent of the syncytial phenotype. We found no correlation between neutralizing activity and anti-fusion activity suggesting that, while gD is involved in cell fusion, it has at least one other function which is required for infectivity.

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Section: Discussionmentioning

confidence: 99%

An Analysis of the Biological Properties of Monoclonal Antibodies against Glycoprotein D of Herpes Simplex Virus and Identification of Amino Acid Substitutions that Confer Resistance to Neutralization

Minson

Hodgman

Digard

et al. 1986

Journal of General Virology

179

183

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“…The function of these genes is not known although one, UL53, is known to be a syn locus (Debroy et aL, 1985). To investigate the role of these putative gene products in the virus life cycle, we attempted to disrupt the four ORFs separately.…”

Section: Discussionmentioning

confidence: 99%

“…UL53 encodes a 338 amino acid polypeptide, with two to four possible transmembrane regions, as well as a potential N-terminal signal sequence. Although no protein product has been identified for UL53, the UL53 open reading frame (ORF) has been shown to be the locus of a mutation causing syncytial plaque morphology (Debroy et al, 1985), suggesting that the gene product may indeed be a membrane protein.…”

Section: Introductionmentioning

confidence: 99%

Investigation of herpes simplex virus type 1 genes encoding multiply inserted membrane proteins

MacLean

Efstathiou

Elliott

et al. 1991

Journal of General Virology

111

106

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The herpes simplex virus type 1 genome contains four open reading frames (ORFs) which are predicted to encode hydrophobic proteins with the potential to cross a membrane several times. The products of these genes (genes UL10, UL20, UL43 and UL53) have not previously been identified. To investigate the role of these proteins in the virus life cycle, we attempted to inactivate the genes individually by inserting the lacZ gene from Escherichia coli within the ORFs. Using this approach we have isolated insertion mutants for UL10 and UL43, as well as a deletion mutant lacking the majority of the UL43 ORF. The growth of the UL10-lacZ virus was slightly impaired in tissue culture compared to that of the wild-type virus parent, whereas the growth of the UL43 mutants was indistinguishable from that of wild-type virus. Furthermore, deletion of the majority of the UL43 ORF did not impair the ability of the virus to replicate in vivo at the periphery, or to spread to and replicate within the nervous system, in a mouse ear model. Repeated attempts to isolate lacZ insertion mutants for UL20 and UL53 were unsuccessful, suggesting that these genes may be essential for virus growth, at least in tissue culture. Using antipeptide sera, the products of genes UL10 and UL20 have been detected.

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“…This sequence is presented in Figure 2 (28). The 51K amino acid sequence possesses low but definite homology with that of the EBV reading frame BBRF3 (27) (27).…”

Section: Methodsmentioning

confidence: 99%

DNA sequence of the region in the genome of herpes simplex virus type 1 containing the exonuclease gene and neighbouring genes

1986

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Nucleotide sequence of a herpes simplex virus type 1 gene that causes cell fusion

Cited by 119 publications

References 52 publications

An Analysis of the Biological Properties of Monoclonal Antibodies against Glycoprotein D of Herpes Simplex Virus and Identification of Amino Acid Substitutions that Confer Resistance to Neutralization

An Analysis of the Biological Properties of Monoclonal Antibodies against Glycoprotein D of Herpes Simplex Virus and Identification of Amino Acid Substitutions that Confer Resistance to Neutralization

Investigation of herpes simplex virus type 1 genes encoding multiply inserted membrane proteins

DNA sequence of the region in the genome of herpes simplex virus type 1 containing the exonuclease gene and neighbouring genes

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