BIOMAT Database Logo BIOMAT Database Logo

Multiepitope polypeptide of the HIV-1 envelope induces neutralizing monoclonal antibodies against V3 loop. 1994

C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
Center for Genetic Engineering and Biotechnology, Havana, Cuba.

A gene encoding a multiepitope polypeptide (MEP) has been synthesized. It contains the information for (1) an 11-amino acid (aa) epitope from the C1 region of gp120 of HIV-1 and (2) 3 epitopes of 15 amino acids each, from the central part of the V3 loop of isolates MN, SC, and WMJII. These four segments are linked by the short spacer peptide AGGGA. This gene was cloned in a plasmid vector and expressed in Escherichia coli as a fusion product with a 62-aa fragment of human IL-2. The recombinant protein TAB1 was purified by washed pellet procedures and reversed-phase HPLC. TAB1 was recognized in ELISAs by 25 of 27 sera from seropositive individuals. Mice were immunized and several hybridomas were obtained. Two of them secrete monoclonal antibodies that react with synthetic peptides from isolates MN, WMJI, WMJIII, and SC with an affinity constant in the range of 10(8) M-1. They also recognized peptides from isolates SF2 and WMJII, but at much lower affinity. The results obtained from peptide ELISAs indicate that the putative epitope recognized by these MAbs lies within the sequence IHIGPGRAFYT. Classic neutralization assays demonstrated that MAb 2C4 neutralizes 50% of the MN isolate at 0.6 micrograms/ml but fails to neutralize IIIB and SF2 strains. The presence of antibodies directed against every one of the component peptides in the sera of rabbits immunized with TAB1 was also documented.

UI MeSH Term Description Entries
D008807 Mice, Inbred BALB C An inbred strain of mouse that is widely used in IMMUNOLOGY studies and cancer research. BALB C Mice, Inbred,BALB C Mouse, Inbred,Inbred BALB C Mice,Inbred BALB C Mouse,Mice, BALB C,Mouse, BALB C,Mouse, Inbred BALB C,BALB C Mice,BALB C Mouse
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
D009500 Neutralization Tests The measurement of infection-blocking titer of ANTISERA by testing a series of dilutions for a given virus-antiserum interaction end-point, which is generally the dilution at which tissue cultures inoculated with the serum-virus mixtures demonstrate cytopathology (CPE) or the dilution at which 50% of test animals injected with serum-virus mixtures show infectivity (ID50) or die (LD50). Neutralization Test,Test, Neutralization,Tests, Neutralization
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010452 Peptide Biosynthesis The production of PEPTIDES or PROTEINS by the constituents of a living organism. The biosynthesis of proteins on RIBOSOMES following an RNA template is termed translation (TRANSLATION, GENETIC). There are other, non-ribosomal peptide biosynthesis (PEPTIDE BIOSYNTHESIS, NUCLEIC ACID-INDEPENDENT) mechanisms carried out by PEPTIDE SYNTHASES and PEPTIDYLTRANSFERASES. Further modifications of peptide chains yield functional peptide and protein molecules. Biosynthesis, Peptide
D010455 Peptides Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are considered to be larger versions of peptides that can form into complex structures such as ENZYMES and RECEPTORS. Peptide,Polypeptide,Polypeptides
D011817 Rabbits A burrowing plant-eating mammal with hind limbs that are longer than its fore limbs. It belongs to the family Leporidae of the order Lagomorpha, and in contrast to hares, possesses 22 instead of 24 pairs of chromosomes. Belgian Hare,New Zealand Rabbit,New Zealand Rabbits,New Zealand White Rabbit,Rabbit,Rabbit, Domestic,Chinchilla Rabbits,NZW Rabbits,New Zealand White Rabbits,Oryctolagus cuniculus,Chinchilla Rabbit,Domestic Rabbit,Domestic Rabbits,Hare, Belgian,NZW Rabbit,Rabbit, Chinchilla,Rabbit, NZW,Rabbit, New Zealand,Rabbits, Chinchilla,Rabbits, Domestic,Rabbits, NZW,Rabbits, New Zealand,Zealand Rabbit, New,Zealand Rabbits, New,cuniculus, Oryctolagus
D011993 Recombinant Fusion Proteins Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes. Fusion Proteins, Recombinant,Recombinant Chimeric Protein,Recombinant Fusion Protein,Recombinant Hybrid Protein,Chimeric Proteins, Recombinant,Hybrid Proteins, Recombinant,Recombinant Chimeric Proteins,Recombinant Hybrid Proteins,Chimeric Protein, Recombinant,Fusion Protein, Recombinant,Hybrid Protein, Recombinant,Protein, Recombinant Chimeric,Protein, Recombinant Fusion,Protein, Recombinant Hybrid,Proteins, Recombinant Chimeric,Proteins, Recombinant Fusion,Proteins, Recombinant Hybrid
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D003001 Cloning, Molecular The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells. Molecular Cloning

Related Publications

C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
Crystal structure of a human rhinovirus that displays part of the HIV-1 V3 loop and induces neutralizing antibodies against HIV-1.
July 2002, Structure (London, England : 1993),
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
Characterization of a Large Panel of Rabbit Monoclonal Antibodies against HIV-1 gp120 and Isolation of Novel Neutralizing Antibodies against the V3 Loop.
January 2015, PloS one,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
Anti-V3 monoclonal antibodies display broad neutralizing activities against multiple HIV-1 subtypes.
April 2010, PloS one,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
Permissive residues within the minimal epitopes of neutralizing monoclonal antibodies to the V3 loop of HIV-1.
July 1996, European journal of immunology,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
A new epitope presenting system displays a HIV-1 V3 loop sequence and induces neutralizing antibodies.
September 1995, Vaccine,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
V3 loop truncations in HIV-1 envelope impart resistance to coreceptor inhibitors and enhanced sensitivity to neutralizing antibodies.
August 2007, PLoS pathogens,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
The V3 loop based multi-epitope polypeptide TAB9 adjuvated with montanide ISA720 is highly immunogenic in nonhuman primates and induces neutralizing antibodies against five HIV-1 isolates.
May 1999, Vaccine,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
A disulfide-bound HIV-1 V3 loop sequence on the surface of human rhinovirus 14 induces neutralizing responses against HIV-1.
March 1999, Biological chemistry,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
A broadly neutralizing macaque monoclonal antibody against the HIV-1 V3-Glycan patch.
October 2020, eLife,
C A Duarte, and M Montero, and A Seralena, and R Valdés, and V Jiménez, and J Benítez, and E Narciandi, and J Madrazo, and G Padrón, and G Sánchez
Focusing the immune response on the V3 loop, a neutralizing epitope of the HIV-1 gp120 envelope.
March 2008, Virology,
Copied contents to your clipboard!