Anti-Variant surface glycoprotein [cAbAn33]

Description:

Recombinant monoclonal antibody to Variant surface glycoprotein. Manufactured using AbAb’s Recombinant Platform with variable regions (i.e. specificity) from the phage display antibody cAbAn33.

Clone Name:

cAbAn33

Published Application(s):

crystallization, SPR, ELISA, FC

Published Species Reactivity:

Trypanosoma

UniProt Accession Number of Target Protein: P26332

Alternative Name(s) of Target: VSG; cAb-An33; cAbAn33_1-0-0; VSG 221; Variant surface glycoprotein MITAT 1.2
Immunogen: The antibody was generated by immunizing a dromedary (Camelus dromedarius) with VSG purified from T. brucei brucei AnTat 1.1. A VHH library was constructed and the antibody was isolated by panning against immobilized AnTat 1.1.

Specificity: The antibody is specific for the conserved carbohydrate moiety on variant surface glycoprotein of the trypanosome coat. The antibody cross-reacts with other VSGs (AnTat 1.1, MITat 1.1, MITat 1.5, and deglycosilated AnTat 1.1).

Application Notes: The antibody specificity and possible cross-reactivity with other VSGs (AnTat 1.1, MITat 1.1, MITat 1.5, and deglycosilated AnTat 1.1) was analyzed via solid-phase ELISA. The antibody recognized all the VSGs. The capacity of cAb-An33 to recognize its epitope on living trypanosomes (AnTat 1.1, MITat 1.1, or MITat 1.5) was analyzed via flow cytometry and microscopy. Flow cytometry showed that the antibody stains parasites of the three VSG classes, although not to the same intensity. Finally, the antibody was fused together with beta-lactamase and employed as a recognition unit in immuno-toxins for trypanosomosis therapy (Stijlemans et al., 2004; PMID: 14527957). The crystal structure of the VHH fragment was determined. The humanized version of the antibody was constructed and the crystal structure determined. The binding affinity of the VHH and the humanized fragments to VSG was measured by surface plasmon resonance (Kd= 28 nM and 539.5 nM respectively) (Conrath et al., 2005; PMID:15913651).

Antibody first published in: Stijlemans et al. Efficient targeting of conserved cryptic epitopes of infectious agents by single domain antibodies. African trypanosomes as paradigm J Biol Chem. 2004 Jan 9;279(2):1256-61. PMID:14527957
Note on publication: The original paper describes the generation and characterization of the antibody.

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