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

Monoclonal antibody neutralization escape mutants of respiratory syncytial virus with unique alterations in the attachment (G) protein.

The Journal of general virology - 1 Mar 1998

Walsh E E, Falsey A R, Sullender W M

Abstract excerpt

Five monoclonal antibody (MAb) neutralization escape mutants of respiratory syncytial virus (RSV) were produced by growing the Long strain RSV (group A virus) in the presence of a neutralizing, group cross-reactive MAb specific for the attachment protein (G). Four viruses (RSV-2, -6, -14 and -15) had amino acid replacements clustered within a highly conserved centrally located 13 amino acid region (position...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Antibodies, Monoclonal

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Base Sequence

Share to Blotting, Western

Share to Molecular Sequence Data

Share to Mutation

Share to Tumor Cells, Cultured

Share to Viral Proteins

Source

Identifiers

PMID: 9519826
DOI: 10.1099/0022-1317-79-3-479

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Monoclonal antibody neutralization escape mutants of respiratory syncytial virus with unique alterations in the attachment (G) protein.PMID 9519826Read ↗

Premature stop codons in the G glycoprotein of human respiratory syncytial viruses resistant to neutralization by monoclonal antibodies.Semantic proximity Read ↗

Contribution of the respiratory syncytial virus G glycoprotein and its secreted and membrane-bound forms to virus replication in vitro and in vivo.Semantic proximity Read ↗

Enhanced neutralization of human respiratory syncytial virus by mixtures of monoclonal antibodies to the attachment (G) glycoprotein.Semantic proximity Read ↗

Antigenic structure of the human respiratory syncytial virus G glycoprotein and relevance of hypermutation events for the generation of antigenic variants.Semantic proximity Read ↗

The three C-terminal residues of human respiratory syncytial virus G glycoprotein (Long strain) are essential for integrity of multiple epitopes distinguishable by antiidiotypic antibodies.Semantic proximity Read ↗

Structure-Based Design and Antigenic Validation of Respiratory Syncytial Virus G Immunogens.Semantic proximity Read ↗

Functional Analysis of Recombinant Respiratory Syncytial Virus Deletion Mutants Lacking the Small Hydrophobic and/or Attachment Glycoprotein GeneSemantic proximity Read ↗

Identification of variable domains of the attachment (G) protein of subgroup A respiratory syncytial virusesSemantic proximity Read ↗

Loss of Conserved Cysteine Residues in the Attachment (G) Glycoprotein of Two Human Respiratory Syncytial Virus Escape Mutants That Contain Multiple A-G Substitutions (Hypermutations)Semantic proximity Read ↗

Antigenic Structure of Human Respiratory Syncytial Virus Fusion GlycoproteinSemantic proximity Read ↗

Multiplex Assay for Detection of Strain-Specific Antibodies against the Two Variable Regions of the G Protein of Respiratory Syncytial VirusSemantic proximity Read ↗

A Respiratory Syncytial Virus Attachment Gene Variant Associated with More Severe Disease in Infants Decreases Fusion Protein Expression, Which May Facilitate Immune Evasion.Semantic proximity Read ↗

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