Using the immunoglobulin G (IgG)

fraction of an antiserum

Using the immunoglobulin G (IgG)

fraction of an antiserum against cell surface proteins of L. reuteri ATCC 53608 (strain 1023), they screened a phage library and identified a number of clones that were reactive with the antiserum and adhered to mucus. Subcloning resulted in the identification of the mub gene, encoding a very large sortase-dependent protein (SDP) with a highly repetitive structure (3000 residues). Domains with the ABT-737 concentration two main types of repeats, that is, Mub1 and Mub2, were shown to adhere to mucus after recombinant expression in Escherchia coli. In another L. reuteri strain, 100-23, a similar approach using an antiserum against the surface proteins was used to identify the lsp (large cell surface protein) gene, which encodes a high molecular mass cell wall protein, Lsp (Walter et al., 2005). Mutational analysis showed a reduced ecological performance of the lsp mutant in the murine gastro intestinal tract (GIT). Boekhorst et al. (2005) performed an in silico search for potential mucus-binding proteins present in several publicly available databases. They reported that a total of 48 proteins containing

at least one MUB domain were identified in 10 lactic acid bacterial species. Callanan et al. (2008) reported that these mucus-binding proteins are involved mainly in GIT colonization as observed from the genome sequence of the Galunisertib solubility dmso dairy isolate L. helveticus DPC4571. A striking difference between the various mucus-binding proteins is the number of repeats of the MUB domain, and it might be interesting to investigate whether the number of repeats correlates with the capacity of binding to mucus (Boekhorst et al., 2006). Buck et al. (2005) reported the genes encoding FbpA, Mub, and SlpA all contribute to the ability of L. acidophilus NCFM to adhere to Caco-2 cells in vitro, confirming that adhesion is determined by multiple factors. mub and fbpA mutations resulted in 65% and 76% decreases in adherence, respectively. In a similar

Fossariinae study, VanPijkeren et al. (2006) mined the genome of L. salivarius UCC118 for the presence of sortase gene homologs and genes encoding SDPs. The sortase gene srtA was deleted, three genes encoding SDPs (large surface protein lspA, lspB, and lspD) were disrupted, and the capacity of adherence of these mutants to HT-29 and Caco-2 cells was investigated. Both the srtA and the lspA mutant showed a significant decrease in adherence. While the adherence of the srtA mutant was on average 50% of wild-type levels, the lspA mutant adhered at around 65%, only slightly better than the Sortase srtA mutant, indicating that LspA plays a key role in adherence to these intestinal cells. Probiotic bacteria have multiple and diverse influences on the host. Different organisms can influence the intestinal luminal environment, epithelial and mucosal barrier function, and the mucosal immune system.

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