Adaptation of the binding domain of S-layer protein as a molecular tag for affinity chromatography development.

Introduction: The S-layer proteins are a class of self-assembling proteins that form bi-dimensional lattices named S-Layer on the cell surface of bacteria and archaea. The protein SlpA, which is the major constituent of the S-layer, contains in its C-terminus region (SlpA), a protein domain (named here as SLAP) responsible for the association of SlpA to the bacterial surface. SLAP was adapted for the development of a novel affinity chromatography method: the SLAP-based affinity chromatography (SAC).

Biochemical and functional characterization of cyclophilins: So similar, yet so different.

spp. are the etiological agent of animal and human brucellosis. We have reported previously that cyclophilins of (CypA and CypB) are upregulated within the intraphagosomal replicative niche and required for stress adaptation and host intracellular survival and virulence.