e Lactobacillus mucosae LM1, isolated from stool samples of a healthy piglet, displays good in vitro mucin adhesion and antimicrobial activity against pathogenic bacteria. To elucidate its antimicrobial effects and to find its epithelial cell and mucin adhesion genes, the genomic sequence of L. mucosae LM1 was investigated.L actobacillus mucosae, found in the mammalian gastrointestinal tract, has been shown to have the ability to adhere to mucosal surfaces (2,3,9). Previous reports have identified L. mucosae as having the ability to attach tightly to the epithelium of the human intestine and to produce antimicrobials and a biofilm when exposed to the physiological conditions of the gut (4). The adhesion of lactobacilli to gastrointestinal mucus makes them a good choice for probiotics since it increases their ability to colonize the gut efficiently, modulate the intestinal immune system, and inhibit pathogenic bacteria (1, 4, 9).L. mucosae LM1 was isolated from stool samples from a healthy piglet (6). Preliminary trials regarding the adhesion and antibacterial activity of L. mucosae LM1 demonstrated good mucin-binding activity in vitro and antibacterial activity against pathogenic bacteria. The genome of L. mucosae LM1 was determined using a Roche 454 GS FLX sequencer and Illumina GA IIx platform. All reads were assembled into 55 contigs by de novo assembly. The initial draft assembly was prepared from the libraries of 22,092,187 reads (950ϫ coverage) using Newbler Assembler 2.3 (Roche), CLC Genomics Workbench 4.8 (CLCbio), and CodonCode Aligner (CodonCode Co.). A functional annotation was performed by the Rapid Annotation using Subsystem Technology (RAST) server and BLASTP-based comparisons with the KEGG and COG databases.The draft genome of L. mucosae LM1 included 2,213,697 bp with a 45.87% GϩC content, 2,039 protein-coding genes, and 56 tRNA-encoding genes. Functions were assigned to 64.6% (1,318) of the total coding sequences; 8.7% (428) were found to be hypothetical proteins that are unique to this strain. A phylogenetic tree produced from the 16S rRNA genes revealed that strain LM1 is most closely related to L. mucosae CCUG 43169 (8). Likewise, 16S rRNA analysis showed strong homology to other Lactobacillus species with completed genomes, including Lactobacillus reuteri DSM 20016 (NCBI reference NC_009513.1), with 94% similarity, and Lactobacillus fermentum IF03956 (GenBank reference AP008937.1), with 95% similarity. The 16S rRNA gene sequence was extracted from whole-genome shotgun assemblies derived from the EzTaxon-e database (5).An analysis of the L. mucosae LM1 genome revealed that LM1 has a specific mucus-binding protein (mub) gene (LBLM1_04370), which showed 95% coverage and 93% similarity to the best-matched L. reuteri mub gene. The mucus-binding activity induced by this mub gene has antimicrobial effects through cell surface protection (7,8). Moreover, the L. mucosae LM1 genome includes a putative ABC transporter and adhesin-like protein (LBLM1_10110) with significant homology (100% coverage and 93...

In this study, a LCH1227 bacterial strain that possesses anti-listerial activity was isolated from fermented food and identified as Lactobacillus salivarius LCH1227 based on its morphological and biochemical properties, as well as its 16S rRNA gene sequences. Anti-listerial substance also inhibited the growth of various Gram-positive bacteria, such as vancomycinresistant Enterococcus faecalis, Streptococcus agalactiae, Bacillus cereus, Lactobacillus fermentum. The highest level of production of antimicrobial substances from L. salivarius LCH1227 occurred during the early stationary phase. The antilisterial activity was found to be stable over a broad range of pH values (2.0-12.0) and after heat treatment. However, it was inactivated by proteolytic enzymes, indicating its proteinaceous nature. The apparent molecular mass of the partially purified anti-listerial substance, as measured by Tricine-SDS-PAGE, was approximately 5 kDa.