ABSTRACT
We generated a novel human neutralizing human mAb RabD4 against rabies virus glycoprotein using in vitro stimulation of human peripheral B cells produced by immunized donor. The human mAb RabD4 showed a high antigen-binding activity and virus-neutralizing activity in the FAVN test with the CVS-11 rabies virus.
Subject(s)
Antibodies, Monoclonal/immunology , Antibodies, Neutralizing/immunology , Antibodies, Viral/immunology , Rabies virus/immunology , Viral Proteins/immunology , HumansABSTRACT
We determined the nucleotide and amino acid sequences of variable domains of three new monoclonal antibodies to the glycoprotein of Ebola virus capsid. The framework and hypervariable regions of immunoglobulin heavy and light chains were identified. The primary structures were confirmed using massspectrometry analysis. Immunoglobulin database search showed the uniqueness of the sequences obtained.
Subject(s)
Antibodies, Monoclonal/chemistry , Antibodies, Viral/chemistry , Ebolavirus/immunology , Immunoglobulin Variable Region/chemistry , Viral Envelope Proteins/chemistry , Amino Acid Sequence , Animals , Antibodies, Monoclonal/genetics , Antibodies, Viral/genetics , Base Sequence , DNA Primers , Electrophoresis , Immunoglobulin Variable Region/genetics , Mice , Viral Envelope Proteins/genetics , Viral Envelope Proteins/immunologyABSTRACT
The monoclonal antibodies to Puumala, Dobrava, Hantaan, and Seoul hantaviruses were obtained using mice. The viruses were known to cause HFRS, and two variants of ELISA were designed. First, Hanta-PUU variant, was constructed using monoclonal antibodies to Puumala virus envelope glycoprotein (G(N):G(C)) for detecting only Puumala virus antigen. The second, Hanta-N variant, was constructed using monoclonal antibodies to Dobrava and Puumala nucleocapsid proteins for detecting four above mentioned hantaviruses. Both Hanta-PUU and Hanta-N assays were reliable in detecting specific hantavirus antigens and the immunogenecity of hantavirus vaccines.
Subject(s)
Antibodies, Monoclonal, Murine-Derived/chemistry , Antigens, Viral/immunology , Hemorrhagic Fever with Renal Syndrome/immunology , Orthohantavirus/immunology , Viral Envelope Proteins/immunology , Viral Vaccines/immunology , Animals , Antibodies, Monoclonal, Murine-Derived/immunology , Chlorocebus aethiops , Enzyme-Linked Immunosorbent Assay/methods , Humans , Mice , Mice, Inbred BALB C , Vero CellsABSTRACT
The peptide conformation in the context of a protein polypeptide chain is influenced by proximal amino acid residues. However, the mechanisms of this interference remain poorly understood. We studied the conformation of angiotensins 1, 2 and 3, which are produced naturally in a sequential fashion from a precursor protein angiotensinogen and contain an identical peptide core structure. Using the example of angiotensins 1, 2 and 3, it was shown that similar amino acid sequences may have significant conformational differences in various molecules. In order to assess the conformational changes, we developed a panel of high-affinity mouse monoclonal antibodies against angiotensins 1, 2 and 3 and studied their cross-reactivity in indirect and competitive ELISAs. It was found that the conformations of inactive angiotensin1 and the corresponding fragment of angiotensinogen are similar; the same is true for the conformations of active angiotensins 2 and 3, whereas the conformations of homologous fragments in the active and inactive angiotensins differ significantly.
