EVAg

Middle East respiratory Syndrome coronavirus (MERS-CoV) was isolated in June 2012 from a man with acute pneumonia and renal failure.

Through direct cloning and expression of the variable heavy chains (VHHs) of HCAbs from the bone marrow of MERS-CoV infected dromedaries, MERS-CoV specific VHHs or nanobodies were produced. VHH-83 binds with exceptionally high affinity to the receptor binding domain of the viral spike protein. In vitro, this VHH efficiently blocks virus entry at picomolar concentrations

HCAb-83 is a MERS-CoV specific camel/human chimeric heavy chain only antibody (HCAb) - composed of the camel VHH-83 linked to a human Fc domain lacking the CH1 exon Through direct cloning and expression of the variable heavy chains (VHHs) of HCAbs from the bone marrow of MERS-CoV infected dromedaries, MERS-CoV specific VHHs or nanobodies were produced. VHH-83 binds with exceptionally high affinity to the receptor binding domain of the viral spike protein. In vitro, HCAb-83 efficiently blocks virus entry at picomolar concentrations

N-terminal domain of the MERS CoV nucleocapsid (1-164). Pure recombinant protein produced in E. coli. resuspended in HEPES buffer 10 mM pH 7.5, NaCl 300 mM.

N-terminal domain of the MERS CoV nucleocapsid (37-164, without the N-terminal intrinsically disordered region. Pure recombinant protein produced in E. coli. resuspended in HEPES buffer 10 mM pH 7.5, NaCl 300 mM