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.

Development of a Salmonella-based oral vaccine to control intestinal colonization of Shiga-toxin-producing Escherichia coli (STEC) in animals.

Shiga-toxin-producing Escherichia coli (STEC) is an important food-borne pathogen that causes hemorrhagic colitis and hemolytic uremic syndrome (HUS) in humans. Since no vaccines are available and antibiotic treatment is not recommended because promotes the appearance of HUS symptoms, the control of STEC intestinal colonization in cows, which is an important environmental reservoir, is crucial to control this zoonosis. Here, we evaluated the adaptation of an attenuated strain of Salmonella enterica serovar Typhimurium (ΔaroA mutant) as a vaccine platform for preventing STEC intestinal colonization that was studied in a mouse model.

Development of an Antigen Delivery Platform Using Decorated With Heterologous Proteins: A Sheep in Wolf's Clothing Story.

S-layers are bacterial structures present on the surface of several Gram-positive and Gram-negative bacteria that play a role in bacterial protection. In ( ATCC 4356), the S-layer is mainly composed of the protein SlpA. A tandem of two copies of the protein domain SLP-A (pfam: 03217) was identified at the C-terminal of SlpA, being this double SLP-A protein domain (in short dSLP-A) necessary and sufficient for the association of the protein to the cell wall.

Two Rieske Fe/S Proteins and TAT System in MAFF303099: Differential Regulation and Roles on Nodulation.

MAFF303099 is a rhizobial strain that nodulates spp. A MAFF303099 mutant strain affected in the gene was generated. This strain presented an altered protein secretion level to the culture supernatant and also a higher sensitivity to SDS.