Intracellular processing of the human respiratory syncytial virus fusion glycoprotein: amino acid substitutions affecting folding, transport and cleavage.

doi:10.1099/0022-1317-73-5-1177

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Article

Intracellular processing of the human respiratory syncytial virus fusion glycoprotein: amino acid substitutions affecting folding, transport and cleavage.

The Journal of general virology - 1 May 1992

Anderson K, Stott E J, Wertz G W

Abstract excerpt

The intracellular processing and transport of the respiratory syncytial virus (RSV) fusion (F) glycoprotein was examined by comparing the maturation and stability of wild-type F, uncleaved mutant F and chimeric F glycoproteins expressed by recombinant vaccinia viruses to that of F protein expressed by RSV. One of the recombinant viruses, vF317, expressed F protein (F317) that was processed like the RSV F...

Topics

Antigens, Viral
Base Sequence
Carrier Proteins
Endoplasmic Reticulum Chaperone BiP
Epitopes
Glycoproteins
HN Protein
Heat-Shock Proteins
Humans
Molecular Chaperones
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Processing, Post-Translational

Recombinant Fusion Proteins

Recombinant Proteins

Respiratory Syncytial Viruses

Sequence Homology, Nucleic Acid

Vaccinia virus

Source

Open in PubMed

Identifiers

PMID: 1375280
DOI: 10.1099/0022-1317-73-5-1177

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1375280-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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