Lactobacillus plantarum for oral peptide delivery

Abstract

The transformed L. lactis, L. brevis, L. johnsonii, L. murinus, and the endogenous murine lactobacillus strain failed to persist in the mouth. Transformed L. plantarum, however, persisted in the mouth and comprised up to 25% of the total lactobacilli at 18 h and 10% at 24 h after feeding. L. plantarum recovered after feeding retained its ability to secrete beta-lactamase into culture medium efficiently. Beta-lactamase activity could be detected in oral secretions at 8 h after feedings. After repeated feedings, however, the L. plantarum containing pKTH2121 gradually lost its ability to persist after feedings. This experiment demonstrates that L. plantarum can transiently colonize the oral mucosa in large numbers, while continuously secreting foreign proteins, raising the possibility of using lactobacilli as a vector for delivery of oral mucosal peptides.

Genome-wide analysis of signal peptide functionality in Lactobacillus plantarum WCFS1

“…So far, engineered secretion in L. plantarum has mostly been based on the use of heterologous signal peptides. The most widely exploited heterologous signal peptides are those from the L. lactis Usp45 protein [ 26 - 28 ], the Streptococcus pyogenes M6 protein [ 5 , 27 , 29 ], and the L. brevis S-layer protein [ 20 , 24 ], as well as signal peptides from different microbial amylases [ 4 , 30 ]. When aiming for the construction of genetically engineered L. plantarum strains for human consumption, there is a need for the use of homologous signal peptides since this limits the use of foreign DNA and since homologous signal peptides may lead to more efficient secretion.…”

Heterologous protein secretion byLactobacillus plantarumusing homologous signal peptides

“…1997; Kerovuo and Tynkkynen 2000) and from the Lactobacillus brevis S‐layer protein (SlpA) (Savijoki et al. 1997; Oh et al. 2007).…”

“…plantarum include SP from the Streptococcus pyogenes M6 protein (Hols et al 1997), from the Lact. amylovorus amylase (Hols et al 1997;Kerovuo and Tynkkynen 2000) and from the Lactobacillus brevis S-layer protein (SlpA) (Savijoki et al 1997;Oh et al 2007). Using a probe vector, Hols et al (1994) were able to isolate chromosomal fragments of Lact.…”

Lactic Acid Bacteria as a Live Delivery System for the in situ Production of Nanobodies in the Human Gastrointestinal Tract

“…Either during or after translocation, a signal peptidase cleaves off the signal peptide and the mature protein is released into the extracellular environment (Schneewind and , 2014). Different signal peptides have been exploited for engineered secretion in LAB, such as that associated with the major lactococcal secreted protein Usp45 (Dieye et al., 2001), the Lactobacillus brevis S-layer protein (SlpA) (Oh et al., 2007), the Streptococcus pyogenes M6 protein (Hols et al., 1997), and the Lactobacillus crispatus aggregation-promoting factor (APF) (Martin et al., 2011; Pant et al., 2011; Gunaydin et al., 2014), among others (Mathiesen et al., 2008). Secreted recombinant proteins can also be engineered by the translational fusion of an anchor peptide (displayed on the bacterial surface) via covalent or non-covalent bonding (Desvaux et al., 2006; Zadravec et al., 2015; Mao et al., 2016; Michon et al., 2016).…”