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Fine mapping and interaction analysis of a linear rabies virus neutralizing epitope
- Source :
- Microbes and Infection. 12:948-955
- Publication Year :
- 2010
- Publisher :
- Elsevier BV, 2010.
-
Abstract
- A novel human antibody AR16, targeting the G5 linear epitope of rabies virus glycoprotein (RVG) was shown to have promising antivirus potency. Using AR16, the minimal binding region within G5 was identified as HDFR (residues 261–264), with key residues HDF (residues 261–263) identified by alanine replacement scanning. The key HDF was highly conserved within phylogroup I Lyssaviruses but not those in phylogroup II. Using computer-aided docking and interaction models, not only the key residues (Asp30, Asp31, Tyr32, Trp53, Asn54, Glu99, Ile101, and Trp166) of AR16 that participated in the interaction with G5 were identified, the van der Waals forces that mediated the epitope–antibody interaction were also revealed. Seven out of eight presumed key residues (Asp30, Asp31, Tyr32, Trp53, Asn54, Glu99, and Ile101) were located at the variable regions of AR16 heavy chains. A novel mAb cocktail containing AR16 and CR57, has the potential to recognize non-overlapping, non-competing epitopes, and neutralize a broad range of rabies virus.
- Subjects :
- Models, Molecular
medicine.drug_class
Immunology
Antibodies, Viral
medicine.disease_cause
Monoclonal antibody
Microbiology
Epitope
Epitopes
medicine
Humans
Conserved Sequence
chemistry.chemical_classification
Alanine
Binding Sites
biology
Linear epitope
Rabies virus
Antibodies, Neutralizing
Virology
Molecular biology
Infectious Diseases
Amino Acid Substitution
chemistry
Docking (molecular)
Mutagenesis, Site-Directed
biology.protein
Antibody
Glycoprotein
Epitope Mapping
Protein Binding
Subjects
Details
- ISSN :
- 12864579
- Volume :
- 12
- Database :
- OpenAIRE
- Journal :
- Microbes and Infection
- Accession number :
- edsair.doi.dedup.....c890cdfeb577b6b3645a0bd3c8d35559