Figure 3 Growth kinetic analyisis of all 13 species of LAB 0–3 days. LAB were grown on MRS agar and changed into new MRS medium and kinetic growth curves were measured in triplicate. All 13 LAB were measured from 0 to 72 hours at 620nanometers. This was performed to discover the different growth phases of the LAB and when each enters early stationary phase. S-Layer proteins (SLP) are one of the most common membrane surface structures in bacteria and make up a large percentage of the total protein content of the bacterial cell, indicating that they are important in structure and/or function [34, 35]. Nevertheless, VX-680 molecular weight the functions of SLPs have been described only hypothetically.

Åvall-Jääskeläinen and Palva (2005) argued that SLPs were involved in protective cell coats, trapping molecules and ions, and acting as structures for adhesion and cell surface recognition [36]. We detected secretion of SLPs only from some lactobacilli (Hma2N, Hma11N, and Bma5N) (Table  2). Each identified SLP contained a conserved SLAP domain determining its surface-layer identification. However, the SLPs that were produced did not form part of a putative operon, but instead were found as single genes in between two other putative operons in the genomes. The putative

operons surrounding the SLP can be seen to follow a specific gene organization, with a gene coding for N-acetyl muramidase and an unidentified cytosolic protein (Figure  SBE-��-CD in vitro 2). We suggest that the SLP in this case may act as a protective layer to inhibit the muramidases destroying the cell wall of the strain

that produced it. Poppinga and colleagues identified medroxyprogesterone an SLP in P.larvae, which causes American foulbrood disease in A. mellifera. They suggested that the pathogens secrete this SLP to aid adherence of the parasite to the bee gut [37]. It has been shown that specific LAB strains can compete for the same receptors in humans as other pathogens in the gastrointestinal tract by competitive exclusion [38, 39]. We know that the LAB symbionts anchor themselves to the crop with structures resembling a mixture of proteins and exo-polysaccharides [15], therefore SLPs may be involved in biofilm formation and take part in the adhesion of the bacteria to the honey crop wall. No S-layer proteins have been annotated in any of the draft Bifidobacterium genomes. Possible reasons for the lack of SLPs in the bifidobacteria might be that they use other mechanisms such as sugars or other lipoproteins for adhesion and protection purposes [40]. The fact that not all of the honeybee LAB symbionts produce these proteins indicates that they are most likely working together in symbiosis to protect themselves in their Autophagy Compound Library cell assay environment. Molecular chaperones (stress proteins) were produced from a number of the LAB symbionts (Table  2).