An anti-HIV-1 gag protein rat monoclonal antibody library. 1995

M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
Laboratoire de Virologie Fondamentale, Université Catholique de Louvain, Brussels, Belgium.

A set of 18 rat monoclonal antibodies (MAbs) directed against human immunodeficiency virus type 1 (HIV-1) gag proteins was derived from 4 independent fusion protocols. The epitopes recognized were delineated using a random fragment expression library representing the whole HIV-1IIIB genome. This panel of rat MAbs was used to analyze the antigenicities of the HIV-1 CAp24 major core protein and the HIV-1 NCp7 nucleocapsid protein. As a result, a limited set of antigenic domains as defined, 3 on CAp24 between amino acids (aa) 195 and 268, 323 and 329, 329 and 352, and one on NCp7 (aa 382-392). Only 4 mouse anti-CAp24 MAbs appeared to recognize the COOH-terminal domain (aa 329-352) defined by the majority of our MAbs. The rat anti-CAp24 (Q1B10) and the rat anti-NCp7 (I5B11) MAbs described here, defined two newly described epitopes, aa 323-329 and aa 382-392.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D012150 Polymorphism, Restriction Fragment Length Variation occurring within a species in the presence or length of DNA fragment generated by a specific endonuclease at a specific site in the genome. Such variations are generated by mutations that create or abolish recognition sites for these enzymes or change the length of the fragment. RFLP,Restriction Fragment Length Polymorphism,RFLPs,Restriction Fragment Length Polymorphisms
D002213 Capsid The outer protein protective shell of a virus, which protects the viral nucleic acid. Capsids are composed of repeating units (capsomers or capsomeres) of CAPSID PROTEINS which when assembled together form either an icosahedral or helical shape. Procapsid,Prohead,Capsids,Procapsids,Proheads
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D000911 Antibodies, Monoclonal Antibodies produced by a single clone of cells. Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal
D000918 Antibody Specificity The property of antibodies which enables them to react with some ANTIGENIC DETERMINANTS and not with others. Specificity is dependent on chemical composition, physical forces, and molecular structure at the binding site. Antibody Specificities,Specificities, Antibody,Specificity, Antibody
D000939 Epitopes Sites on an antigen that interact with specific antibodies. Antigenic Determinant,Antigenic Determinants,Antigenic Specificity,Epitope,Determinant, Antigenic,Determinants, Antigenic,Specificity, Antigenic
D001483 Base Sequence The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence. DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D014764 Viral Proteins Proteins found in any species of virus. Gene Products, Viral,Viral Gene Products,Viral Gene Proteins,Viral Protein,Protein, Viral,Proteins, Viral

Related Publications

M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
December 1993, FEBS letters,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
December 2011, Antiviral research,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
September 2010, The Journal of antimicrobial chemotherapy,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
August 1990, Journal of immunological methods,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
June 1988, Journal of virological methods,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
October 2003, Virology,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
December 1997, Cell,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
August 1999, Hybridoma,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
July 2016, Oncotarget,
M Bodéus, and M Heusterspreute, and F Hirsch, and R Benarous, and H Bazin, and G Burtonboy
January 1993, Biochimica et biophysica acta,
Copied contents to your clipboard!