Polymer Adhesin Domains in Gram-Positive Cell Surface Proteins

Abstract

Surface proteins in Gram-positive bacteria are often involved in biofilm formation, host-cell interactions, and surface attachment. Here we review a protein module found in surface proteins that are often encoded on various mobile genetic elements like conjugative plasmids. This module binds to different types of polymers like DNA, lipoteichoic acid and glucans, and is here termed polymer adhesin domain. We analyze all proteins that contain a polymer adhesin domain and classify the proteins into distinct classes based on phylogenetic and protein domain analysis. Protein function and ligand binding show class specificity, information that will be useful in determining the function of the large number of so far uncharacterized proteins containing a polymer adhesin domain.

Growth fitness, heme uptake and genomic variants in mutants of oxygen-tolerant Lacticaseibacillus casei and Lactiplantibacillus plantarum strains

“…The genome of N87-AE284 harbours a nucleotide transition in LPXTGmotif cell wall anchor domain-containing protein. Cell surface proteins with a LPXTG-like motif are involved in the adhesion capability of LAB (Järvå et al, 2020) and, therefore, further investigation should be carried-out to verify the real impact of this mutation on some strain features (e.g. growth, cellular adhesion, biofilm formation).…”

Advances of genetic engineering in streptococci and enterococci

“…A transcriptional regulator, which is encoded by the pheromone‐responsive plasmid, binds to the pheromone peptide and then up‐regulates expression of the conjugation operon type IV secretion system 14‐16 . A member of the pheromone‐induced genes, aggregation substance, is expressed on the donor cell surface to form a tightly packed aggregate with a mixture of multiple donor and recipient cells, allowing for highly efficient plasmid transfer even in liquid‐phase culture 17‐19 . For the induction of plasmid conjugative transfer, five variants of the responsive plasmids pAD1, pPD1, pCF10, pAM373, and pOB1 have been identified with the specific pheromone peptides cAD1 (LFSLVLAG), cPD1 (FLVMFLSG), cCF10 (LVTLVFV), cAM373 (AIFILAS), and cOB1 (VAVLVLGA) 14,20 .…”

“…[14][15][16] A member of the pheromone-induced genes, aggregation substance, is expressed on the donor cell surface to form a tightly packed aggregate with a mixture of multiple donor and recipient cells, allowing for highly efficient plasmid transfer even in liquid-phase culture. [17][18][19] For the induction of plasmid conjugative transfer, five variants of the responsive plasmids pAD1, pPD1, pCF10, pAM373, and pOB1 have been identified with the specific pheromone peptides cAD1 (LFSLVLAG), cPD1 (FLVMFLSG), cCF10 (LVTLVFV), cAM373 (AIFILAS), and cOB1 (VAVLVLGA). 14,20 Based on these facts about enterococcal pheromone-responsive conjugative plasmids, Kristich et al developed a highly efficient conjugation-based allele exchange approach for E. faecalis.…”

Structural foundation for the role of enterococcal PrgB in conjugation, biofilm formation and virulence

“…PrgA is a conjugation regulator that provides surface exclusion to prevent unwanted conjugation. We have previously shown that PrgA consists of a protease domain that is presented far away from the cell wall via a long stalk and that it’s likely mediating the proteolytic cleavage of PrgB 15,16 . PrgC is a virulence factor, but its function and structure remain unknown 17 .…”

“…1B). As all described polymer adhesin domains, PrgB has a central ridge with a conserved cation binding site 16,33 . In the homologous GbpC, from Streptococcus mutans , this site has been suggested to bind glucans 34 .…”