Structural and Functional Analysis of the S-layer Protein Crystallisation Domain of Lactobacillus acidophilus ATCC 4356: Evidence for Protein–Protein Interaction of two Subdomains

Genetic analysis of Bacillus anthracis Sap S-layer protein crystallization domain

“…These were large polypeptides, showing that this two-hybrid system can accommodate such fragments. The requirement for large polypeptides to drive the Sap c interaction may be characteristic of S-layer protein assembly, as biochemical analyses carried out on other S-layer proteins showed that large polypeptides are required for crystallization and selfassembly (Jarosch et al, 2001;Sillanpää et al, 2000;Smit et al, 2002). Three-dimensional crystallography has never been successfully applied to complete S-layer proteins.…”

“…The other domain appears to be a crystallization domain (Bingle et al, 1987;Mesnage et al, 1997Mesnage et al, , 1999Howorka et al, 2000;Jarosch et al, 2001;Smit et al, 2002;Mader et al, 2004). Recent studies have focused on the structurefunction relationships of this domain.…”

“…Recent studies have focused on the structurefunction relationships of this domain. Mutagenesis approaches, be they point mutations or deletions, have identified regions within the crystallization domain that are critical for array assembly (Howorka et al, 2000;Sillanpää et al, 2000;Jarosch et al, 2001;Smit et al, 2002). However, these analyses have not provided an overall picture of how an S-layer protein self-assembles to generate an ordered array.…”

“…However, these analyses have not provided an overall picture of how an S-layer protein self-assembles to generate an ordered array. A conclusion is that only small portions of the crystallization domain can generally be deleted before its capacity to self-assemble is lost (Sillanpää et al, 2000;Jarosch et al, 2001;Smit et al, 2002). Only a few research groups have carried out structural analysis of S-layer protein crystallization (Claus et al, 2002;Jing et al, 2002;Pavkov et al, 2003), and the atomic structure remains unknown.…”

Exploring Surface Display Technology for Enhancement of Delivering Viable Lactic Acid Bacteria to Gastrointestinal Tract

“…The (lipo)teichoic acids were identified as the cell wall ligands of SA and CbsA. Moreover, the specific cell wall component that interacts with SlpA was shown to be the neutral polysaccharide moiety of the cell wall (Antikainen et al, 2002;Avall-Jaaskelainen et al, 2008;Smit et al, 2002). Avall-Jaaskelainen (2002) decribed the construction of recombinant L. brevis strains expressing poliovirus epitope VP1 of 10 amino acid residues inserted in the slpA gene.…”