Identification and Characterization of Domains Responsible for Cell Wall Binding, Self-Assembly, and Adhesion of S-layer Protein from Lactobacillus acidophilus CICC 6074

Lactobacillus S-layer protein (SLP) is a biologically active protein on the cell surface. To further elucidate the structures and functions of SLP in Lactobacillus acidophilus CICC 6074, this study was conducted to identify the functional domains of SLP which is responsible for cell wall anchoring, self-assembly, and adhesion. The gene (slpA) of L. acidophilus CICC 6074 SLP was amplified by polymerase chain reaction and speculated functional domains. Fusion proteins of C-terminal truncations from SLP were exogenously expressed in Escherichia coli BL21 (DE3). FITC-labeling N-terminal truncations of SLP were synthesized. The C -terminal domain was more likely to be the binding region, and the cell wall-anchored receptor of SLP was teichoic acid. Furthermore, N-terminal truncations could self-assemble to milk fat globule membrane polar lipid liposomes observed using a fluorescence microscope. Notably, SAN1 (region 32-55) of N-terminal truncations was mainly responsible for the adhesion of SLP to HT-29 cells. These results showed that SLP played a crucial role in the functions of L. acidophilus CICC 6074, which might be of significant reference value for future studies.

Automated summary

This study identified the functional domains of S-layer protein (SLP) in Lactobacillus acidophilus CICC 6074, revealing the binding region in the C-terminal domain and the cell wall-anchored receptor as teichoic acid. N-terminal truncations of SLP were found to self-assemble into milk fat globule membrane polar lipid liposomes, and the SAN1 region was responsible for the adhesion of SLP to HT-29 cells.