RRC ID 60262
Author Fina Martin J, Palomino MM, Cutine AM, Modenutti CP, Fernández Do Porto DA, Allievi MC, Zanini SH, Mariño KV, Barquero AA, Ruzal SM.
Title Exploring lectin-like activity of the S-layer protein of Lactobacillus acidophilus ATCC 4356.
Journal Appl Microbiol Biotechnol
Abstract 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 the adherence of bacteria to host cells. We have previously described that the S-layer protein of L. acidophilus possesses anti-viral and anti-bacterial properties. In this work, we extracted and purified S-layer proteins from L. acidophilus ATCC 4356 cells to study their interaction with cell wall components from prokaryotic (i.e., peptidoglycan and lipoteichoic acids) and eukaryotic origin (i.e., mucin and chitin), as well as with viruses, bacteria, yeast, and blood cells. Using chimeric S-layer fused to green fluorescent protein (GFP) from different parts of the protein, we analyzed their binding capacity. Our results show that the C-terminal part of the S-layer protein presents lectin-like activity, interacting with different glycoepitopes. We further demonstrate that lipoteichoic acid (LTA) serves as an anchor for the S-layer protein. Finally, a structure for the C-terminal part of S-layer and possible binding sites were predicted by a homology-based model.
Volume 103(12)
Pages 4839-4857
Published 2019-6-1
DOI 10.1007/s00253-019-09795-y
PII 10.1007/s00253-019-09795-y
PMID 31053916
IF 3.67
Times Cited 1
General Microbes JCM5818