Discover Community Create You

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

Article

Mutations in the conserved carboxy-terminal hydrophobic region of glycoprotein gB affect infectivity of herpes simplex virus.

The Journal of general virology - 1 Dec 1999

Wanas Essam, Efler Sue, Ghosh Kakoli, Ghosh Hara P

Abstract excerpt

Glycoprotein gB is the most highly conserved glycoprotein in the herpesvirus family and plays a critical role in virus entry and fusion. Glycoprotein gB of herpes simplex virus type 1 contains a hydrophobic stretch of 69 aa near the carboxy terminus that is essential for its biological activity. To determine the role(s) of specific amino acids in the carboxy-terminal hydrophobic region, a number of amino acids...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Conserved Sequence
Share to COS Cells
Share to Dimerization

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescent Antibody Technique

Share to Genetic Complementation Test

Share to Herpesvirus 1, Human

Share to Viral Envelope Proteins

Share to Virion

Source

Identifiers

PMID: 10567651
DOI: 10.1099/0022-1317-80-12-3189

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations in the conserved carboxy-terminal hydrophobic region of glycoprotein gB affect infectivity of herpes simplex virus.PMID 10567651Read ↗

Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity.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 ↗

Alanine substitution of conserved residues in the cytoplasmic tail of herpes simplex virus gB can enhance or abolish cell fusion activity and viral entry.Semantic proximity Read ↗

Structure-Based Mutations in the Herpes Simplex Virus 1 Glycoprotein B Ectodomain Arm Impart a Slow-Entry Phenotype.Semantic proximity Read ↗

Function of glycoprotein B homologues of the family herpesviridae.Semantic proximity Read ↗

The Neutralizing Linear Epitope of Human Herpesvirus 6A Glycoprotein B Does Not Affect Virus Infectivity.Semantic proximity Read ↗

Fusion-deficient insertion mutants of herpes simplex virus type 1 glycoprotein B adopt the trimeric postfusion conformation.Semantic proximity Read ↗

Effects of truncation of the carboxy terminus of pseudorabies virus glycoprotein B on infectivity.Semantic proximity Read ↗

Mutational dissection of HCMV gB and gH cytoplasmic tails highlights conserved and divergent features of fusion regulation.Semantic proximity Read ↗

Restoration of function of carboxy-terminally truncated pseudorabies virus glycoprotein B by point mutations in the ectodomain.Semantic proximity Read ↗

Herpes simplex virus type 1 glycoprotein B requires a cysteine residue at position 633 for folding, processing, and incorporation into mature infectious virus particles.Semantic proximity Read ↗

Functional dissection of HCMV gB's autonomous fusion activity provides insights into how polymorphisms in clinical isolates confer distinct characteristics.Semantic proximity Read ↗

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