Sequenced from human samples with prior exposure to equine Hendra virus (HeV) vaccine, targeting distinct antigenic sites.
≥ 5.0 mg/ml
≤ 1.0 EU/mg as determined by the LAL method
≥95% monomer by analytical SEC
This recombinant monoclonal antibody is aseptically packaged and formulated in 0.01 M phosphate buffered saline (150 mM NaCl) PBS pH 7.2 - 7.4 with no carrier protein, potassium, calcium or preservatives added.
Functional grade preclinical antibodies are manufactured in an animal free facility using only In vitro protein free cell culture techniques and are purified by a multi-step process including the use of protein A or G to assure extremely low levels of endotoxins, leachable protein A or aggregates.
Storage and Handling
Functional grade preclinical antibodies may be stored sterile as received at 2-8°C for up to one year. For longer term storage, aseptically aliquot in working volumes without diluting and store at ≥ -70°C. Avoid Repeated Freeze Thaw Cycles.
Country of Origin
Standard Overnight on Blue Ice.
Other Applications Reported In Literature ?
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.
HENV-103 activity is directed against an area spanning the β1 and β6 propeller blades of receptor binding protein (RBP).
Henipavirus RBP is an envelope glycoprotein.
Henipavirus spp. are enveloped, single-stranded RNA viruses in the family Paramyxovirus1. Five species have been identified, two of which, Hendra virus (HeV) and Nipah virus (NiV), are highly virulent emerging pathogens with high case-fatality ratios. The other three species, Cedar virus, Ghanaian bat virus, and Mojiang virus are not known to cause human disease. Pteropid bats are the reservoir host. HeV is transmitted by direct contact with infected horses, their fluids, or tissues1. Horses are infected by exposure to pteropid bats. NiV is transmitted by contact with infected pigs or bats and person-to-person. Both HeV and NiV cause severe influenza-like illness that can progress to encephalitis.
Potently neutralizing antibodies to HeV and/or NiV have been identified2, 3, 4, 5. HENV-103 was isolated from circulating B cells of an individual exposed to equine HeV vaccine5. Peripheral blood mononuclear cells were tested for binding to recombinant forms of the receptor binding protein (RBP) of NiVB, NiVM, or HeV. The mAb panel grouped into at least six distinct antigenic sites, A-F. HENV-103, group D, binds recombinant RBP and neutralizes HeV, NiVM, and NiVB.. HENV-103 maps to a distinct site on the HeV-RPB head domain spanning the β1 and β6 propeller blades, a region at the interface between protomers within the dimer-of-dimers structure of the HeV-RBP tetramer, suggesting a semi-cryptic site of vulnerability. nsEM mapping shows that HENV-103 binds at the putative dimeric interface. Binding of HENV-103 to RBP is enhanced by ephrin-B2.
References & Citations
1. Aguilar HC, Ataman ZA, Aspericueta V, et al. J Biol Chem. 284(3):1628-1635. 2009.
2. Mire CE, Chan YP, Borisevich V, et al. J Infect Dis. 221(Suppl 4):S471-S479. 2020.
3. Zhu Z, Dimitrov AS, Bossart KN, et al. J Virol. 80(2):891-899. 2006.
4. Doyle MP, Kose N, Borisevich V, et al. Cell Rep. Aug 31;36(9):109628. 2021.
Products are for research use only. Not for use in diagnostic or therapeutic procedures.