Find in Library

Many <i>Lactobacillus casei</i> strains are reported to exhibit anti-proliferative effects on colorectal cancer cells; however, the mechanism remains largely unknown. While there has been considerable interest in bacterial small metabolites such as short chain fatty acids, prior reports suggested that larger-sized molecules mediate the anti-proliferative effect of <i>L. casei</i>. Here, other possible ways of communication between gut bacteria and its host are investigated. LevH1 is a protein displayed on the surface of <i>L. casei</i>, and its mucin binding domain is highly conserved. Based on previous reports that the cell-free supernatant fractions decreased colorectal cell proliferation, we cloned the mucin binding domain of the LevH1 protein, expressed and purified this mucin binding protein (MucBP). It has a molecular weight of 10 kDa, is encoded by a 250 bp gene, and is composed primarily of a β-strand, β-turns, and random coils. The amino acid sequence is conserved while the 36th amino acid residue is arginine in <i>L. casei</i> CAUH35 and serine in <i>L. casei</i> IAM1045, LOCK919, 12A, and Zhang. MucBP^36R exhibited dose-dependent anti-proliferative effects against HT-29 cells while a mutation of 36S abolished this activity. Predicted structures suggest that this mutation slightly altered the protein structure, thus possibly affecting subsequent communication with HT-29 cells. Our study identified a novel mode of communication between gut bacteria and their host.