Evaluation of human and non-human primate antibody binding to pig cells lacking GGTA1/CMAH/β4GalNT2 genes.

ABSTRACT:

Background

Simultaneous inactivation of pig GGTA1 and CMAH genes eliminates carbohydrate xenoantigens recognized by human antibodies. The β4GalNT2 glycosyltransferase may also synthesize xenoantigens. To further characterize glycan-based species incompatibilities, we examined human and non-human primate antibody binding to cells derived from genetically modified pigs lacking these carbohydrate-modifying genes.

Methods

The Cas9 endonuclease and gRNA were used to create pigs lacking GGTA1, GGTA1/CMAH, or GGTA1/CMAH/β4GalNT2 genes. Peripheral blood mononuclear cells were isolated from these animals and examined for binding to IgM and IgG from humans, rhesus macaques, and baboons.

Results

Cells from GGTA1/CMAH/β4GalNT2 deficient pigs exhibited reduced human IgM and IgG bi

SUBMITTER: Estrada JL 

PROVIDER: S-EPMC4464961 | biostudies-literature | 2015 May-Jun

REPOSITORIES: biostudies-literature