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

doi:10.1128/jvi.78.3.1540-1551.2004

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

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

Journal of virology - 1 Feb 2004

Beitia Ortiz de Zarate Igor, Kaelin Karin, Rozenberg Flore

Abstract excerpt

Herpes simplex virus type 1 (HSV-1) is a human pathogen of the alphaherpesvirus family which infects and spreads in the nervous system. Glycoproteins play a key role in the process of assembly and maturation of herpesviruses, which is essential for neuroinvasion and transneuronal spread. Glycoprotein B (gB) is a main component of the HSV-1 envelope and is necessary for the production of infectious particles. The...

Topics

Amino Acid Motifs
Amino Acid Sequence
Animals
Biological Transport
COS Cells
Cell Line
Chlorocebus aethiops
Cytoplasm
Endocytosis
Genetic Complementation Test
Green Fluorescent Proteins
Herpesvirus 1, Human
Humans

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.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Luminescent Proteins

Molecular Sequence Data

Mutation

Protein Processing, Post-Translational

Recombinant Fusion Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 14722308
DOI: 10.1128/jvi.78.3.1540-1551.2004
PMCID: PMC321396

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.