Exploring lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC4356 (FMJ AND MMP equally contribution)

JOAQUINA FINA MARTIN* AMBOS AUTORES CONTRIBUYERON EQUIVALENTEMENTE; MARÍA MERCEDES PALOMINO* AMBOS AUTORES CONTRIBUYERON EQUIVALENTEMENTE; CUTINE AM; MODENUTTI C; DARÍO FERNANDEZ DO PORTO; ALLIEVI MARIANA C; ZANINI SH; MARIÑO KV; BARQUERO A; RUZAL SANDRA M.

APPLIED MICROBIOLOGY AND BIOTECHNOLOGY

SPRINGER

Lugar: Berlin; Año: 2019

0175-7598

The surface layer (S-layer) protein of Lactobacillus acidophilus is a crystalline array of self-assembling, proteinaceous subunits non-covalently bound to the outmost bacterial cell wall envelope and is involved in adherence of bacteria to host cells. We have previously described that the S-layer protein of Lactobacillus acidophilus possesses antiviral and antibacterial properties. In this work, we extracted and purified S-layer proteins from Lactobacillus acidophilus ATCC 4356 cells to study their interaction with prokaryotic (i.e. peptidoglycan and lipoteichoic acids) and eukaryotic (i.e. mucin and chitin) macromolecules, as well as with viruses, bacteria, yeast and blood cells. Our results show that the C-terminal portion of the S-layer protein presents lectin-type activity, interacting with different glycoepitopes. We further demonstrate that lipoteichoic acid serves as a receptor for the S-layer protein. Finally, a structure for the C-terminal portion of S-layer and possible binding sites were predicted by a homology-based model.Running Title: S-layer protein of Lactobacillus carbohydrate interaction