EVAg

Linear peptide epitopes within SARS-CoV-2 orf6 protein (#1: aa 44 - 58, #2: aa 38-52). The peptides are fused to a multimeric protein scaffold based on Lumazine Synthase. The particles were expressed in E.coli and purified by FLAG-affinity chromatography.

The full-length genome of TYLCV (1.7 copies) is cloned in the binary plasmid vector pCambia 0380, allowing transformation into Agrobacterium and infection of plants.

The full-length genome of TYLCV-Mld (2 copies in tandem) is cloned in the binary plasmid vector pCambia 2300 allowing transformation into Agrobacterium and infection of plants

The full-length genome of PYMV-A (1.44 copies) is cloned in the binary plasmid vector pCambia 0380 allowing transformation into Agrobacterium and infection of plants

The full-length genome of PYMV-B component (1.54 copies) is cloned in the binary plasmid vector pCambia 0380, allowing transformation into Agrobacterium and infection of plants

The full-length genome of Tomato leaf curl Comoros virus(1.2 copies) is cloned in the binary plasmid vector pCambia 2300, allowing transformation into Agrobacterium and infection of plants

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