Anti-Japanese Encephalitis Virus (Clone: JEV-75) – Purified No Carrier Protein

A panel of human mAbs against JEV, including JEV-75, was generated from donors immunized with a GIII vaccine strain (JEV-SA14-14-2)².

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. Due to inherent biochemical properties of antibodies, certain products may be prone to precipitation over time. Precipitation may be removed by aseptic centrifugation and/or filtration.

Recombinant 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.

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.

Standard Overnight on Blue Ice.

ELISA
N: JEV-75 completely protects against lethal JEV-Nakayama (GIII) infection when administered as prophylaxis in a mouse challenge model and provides significant protection against both JEV-Nakayama (GIII) and JEV-2372/79 (GI) strains when administered 5 days post-infection². Furthermore, focus reduction neutralization tests of JEV-75 against vaccine strain SA14-14-2 [GIII] and prototype strains 2372/79 [GI], MAR 859 [GI], Bennett [GII], SA14 [GIII], Nakayama [GIII], and JKT 7887 [GIV] show strong neutralizing activity against GI, GII, and GIII strains and no inhibition of the GIV strain. JEV-75 neutralizes in both pre- and post-attachment assays and moderately inhibits fusion at the plasma membrane in a fusion-from-without assay.

JEV-75 activity is directed against the E ectodomain, but not to E-DI or E-DIII. Furthermore, this human Mab showed no cross-reactivity to West Nile Virus or Zika Virus E proteins.

JEV-75 binds to the E ectodomain but not to DI or DIII². Alanine scanning mutagenesis at sites corresponding to the E ectodomain cause loss-of-binding at S275 in the DI-DII-hinge region, L180 in the DI-LR, N82 in the DII-LR, W217 in the DII-central interface, and DIII residue F308 in the A-strand epitope.

Japanese Encephalitis Virus (JEV) is a mosquito-borne, enveloped, positive-stranded RNA virus in the Flavivirus genus endemic to Asia and parts of the western Pacific¹. Symptomatic JEV infection is most common in children in areas of endemicity or travellers to those regions. Severe symptoms occur in ~1% of cases, with a case-fatality ratio of 20–30%. Survivors often have serious neurologic, cognitive, or psychiatric sequelae. Five JEV genotypes have been identified and existing vaccines are derived from historically predominant GIII strains².

1. Hills SL, Lindsey NP, Fischer M. Chapter 4: Travel-Related Infectious Diseases, Japanese Encephalitis. In: Brunette GW, Nemhauser JB, eds. 2020 CDC Yellow Book. CDC; National Center for Emerging and Zoonotic Infectious Diseases (NCEZID), Division of Global Migration and Quarantine (DGMQ), Link Text

2. Fernandez E, Kose N, Edeling MA, et al. mBio. 9(1):e00008-18. 2018.