Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity.

doi:10.1006/viro.1994.1098

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity.

Virology - 15 Feb 1994

Dean H J, Terhune S S, Shieh M T, Susmarski N, Spear P G

Abstract excerpt

Previous studies have shown that cell-associated herpes simplex virus (HSV) glycoprotein gD can interfere with infection of the cells by HSV and other alphaherpesviruses and that HSV mutants resistant to this gD-mediated interference can be isolated. Here we report that HSV mutants selected for resistance to gD-mediated interference are altered in specific infectivity for cells that do not express gD. Two...

Topics

Amino Acid Sequence
Amino Acids
Animals
Base Sequence
Blotting, Western
CHO Cells
Cell Line
Cells, Cultured
Cricetinae
DNA, Viral
Humans

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molecular Sequence Data

Mutation

Neutralization Tests

Phenotype

Sequence Homology, Amino Acid

Simplexvirus

Viral Envelope Proteins

Source

Open in PubMed

Identifiers

PMID: 8116256
DOI: 10.1006/viro.1994.1098

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-8116256-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Single amino acid substitutions in gD of herpes simplex virus 1 confer resistance to gD-mediated interference and cause cell-type-dependent alterations in infectivity.PMID 8116256Read ↗

Partial resistance to gD-mediated interference conferred by mutations affecting herpes simplex virus type 1 gC and gK.Semantic proximity Read ↗

Modified entry and syncytium formation by herpes simplex virus type 1 mutants selected for resistance to heparin inhibition.Semantic proximity Read ↗

Structural Domains of the Herpes Simplex Virus 1 gD Protein That Restrict Human Immunodeficiency Virus Particle InfectivitySemantic proximity Read ↗

Pseudotyping of glycoprotein D-deficient herpes simplex virus type 1 with vesicular stomatitis virus glycoprotein G enables mutant virus attachment and entry.Semantic proximity Read ↗

Glycoprotein D of herpes simplex virus encodes a domain which precludes penetration of cells expressing the glycoprotein by superinfecting herpes simplex virus.Semantic proximity Read ↗

Mutations in herpes simplex virus glycoprotein D distinguish entry of free virus from cell-cell spread.Semantic proximity Read ↗

Deletions in herpes simplex virus glycoprotein D define nonessential and essential domains.Semantic proximity Read ↗

Glycoprotein targeted therapeutics: a new era of anti‐herpes simplex virus‐1 therapeuticsSemantic proximity Read ↗

Herpes simplex virus infects most cell types in vitro: clues to its successSemantic proximity Read ↗

An analysis of the in vitro and in vivo phenotypes of mutants of herpes simplex virus type 1 lacking glycoproteins gG, gE, gI or the putative gJ.Semantic proximity Read ↗

Herpes Simplex Virus Glycoprotein B Mutations Define Structural Sites in Domain I, the Membrane Proximal Region, and the Cytodomain That Regulate Entry.Semantic proximity Read ↗

The role of herpes simplex virus glycoproteins in the virus replication cycle.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.