S-layer proteins as immune players: Tales from pathogenic and non-pathogenic bacteria

Assandri, Matías Hernán; Malamud, Mariano; Trejo, Fernando Miguel; Serradell, María de los Ángeles

doi:10.1016/j.crmicr.2023.100187

Cited by 3 publications

(2 citation statements)

References 125 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In summary, the detailed atomic structure of Lactobacillus S-layer proteins, SlpA and SlpX, reveals essential domain swapping for SlpX integration and indicates self-assembly model for the main SLP, that is in line with prior studies. This structure not only aids in identifying key surface areas for host interactions but also paves the way for using S-layer proteins or engineered lactobacili in therapeutic applications, such as treating in ammatory diseases and vaccine development 55 . Additionally, understanding the S-layer's attachment to teichoic acids represents a foundation for novel strategies in combating infectious and bacteria-mediated in ammation processes for pathogenic bacteria containing LTA in the cell wall.…”

Section: Ta Binding Areas Are Conserved Among Lactobacillimentioning

confidence: 99%

The molecular architecture of Lactobacillus S-Layer: Assembly and attachment to teichoic acids

Sagmeister,

Gubensäk,

Buhlheller

et al. 2024

Preprint

View full text Add to dashboard Cite

S-layers are crystalline arrays found on bacterial and archaeal cells. Lactobacillus is a diverse family of bacteria known especially for potential gut health benefits. This study focuses on the S-layer proteins from Lactobacillus acidophilus and Lactobacillus amylovorus common in the mammalian gut. Atomic resolution structures of Lactobacillus S-layer proteins SlpA and SlpX exhibit domain swapping and the obtained assembly model of the main S-layer protein SlpA aligns well with prior electron microscopy and mutagenesis data. The S-layer's pore size suggests a protective role, with charged areas aiding adhesion. A highly similar domain organization and interaction networks is observed across the Lactobacillus genus. Interaction studies revealed conserved binding areas specific for attachment to teichoic acids. The structure of the SlpA S-layer and the suggested incorporation of SlpX, as well as its interaction with teichoic acids lays the foundation for deciphering its role in immune responses and for developing effective treatments for a variety of infectious and bacteria-mediated inflammation processes, opening new opportunities for targeted engineering of the S-layer or lactobacilli bacteria in general.

show abstract

Section: Ta Binding Areas Are Conserved Among Lactobacillimentioning

confidence: 99%

The molecular architecture of Lactobacillus S-Layer: Assembly and attachment to teichoic acids

Sagmeister,

Gubensäk,

Buhlheller

et al. 2024

Preprint

View full text Add to dashboard Cite

show abstract

“…Previously isolated four strains of Levilactobacillus brevis MB1, MB2, MB13, and MB20, are capable of producing S-proteins, as demonstrated after proteomic analysis and trypsinization followed by liquid chromatography-mass spectrometry (LC-MS) and Mascot search (Banić et al, 2022). Surface (S)-layer proteins (S-proteins) are two-dimensional, paracrystalline, monomolecular crystalline structures of surface (glyco)proteins that cover the cell surface of hundreds of different species of almost all taxonomic groups of Grampositive and Gram-negative bacteria and archaea in the form of a layer (S-layer) (Assandri et al, 2023). As the outermost layer covering the surface of the cell, the S-protein layer is in direct contact with its microenvironment, and the role of S-proteins can be studied from two different approaches -their role in the adhesion of bacteria to various surfaces and substrates and their role as a mechanical barrier in a harmful environment (Gerbino et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

S-layer proteins in microencapsulated freeze-dried probiotic Levilactobacillus brevis strains

Čuljak

2024

Mljekarstvo

View full text Add to dashboard Cite

The presence of surface (S)-layer proteins as a rare property of lactic acid bacteria plays an important role in the expression of the probiotic properties of the producer strain and protects the cells from unfavourable environmental conditions. Therefore, the aim of this work was to evaluate the role of S-layer proteins of four Levilactobacillus brevis MB1, MB2, MB13, and MB20 strains, previously isolated from human milk. The results showed better survival under simulated gastrointestinal tract (GIT) conditions and better adhesion to Caco-2 cells, achieved when S-proteins were present on the surface of the examined probiotic Levilactobacillus brevis strains. Free cells and cells microencapsulated in alginate, with or without galactooligosaccharides (GOS) and fructooligosaccharides (FOS), survived in high numbers during freeze-drying and one-month storage at 4 °C, as well as during exposure to simulated GIT conditions (>108 CFU/g), thus fulfilling the primary technological criterion for the selection of probiotic strains. Higher survival of freeze-drying of encapsulated cells than free cells, can be attributed to the protective effect of alginate, GOS and FOS as prebiotic agents. However, GOS was more protective than FOS in maintaining the viability of microencapsulated Levilactobacillus brevis MB1, MB2, MB13 and MB20 cells in alginate during storage and under the harsh conditions of GIT and freeze-drying.

show abstract

Cryo-EM structure and polar assembly of the PS2 S-layer ofCorynebacterium glutamicum

Sogues,

Sleutel,

Petit

et al. 2024

Preprint

View full text Add to dashboard Cite

The polar-growing Corynebacteriales have a complex cell envelope architecture characterized by the presence of a specialized outer membrane composed of mycolic acids. In some Corynebacteriales, this mycomembrane is further supported by a proteinaceous surface layer or ‘S-layer’, whose function, structure and mode of assembly remain largely enigmatic. Here, we isolatedex vivoPS2 S-layers from the industrially importantCorynebacterium glutamicumand determined its atomic structure by 3D cryoEM reconstruction. PS2 monomers consist of a six-helix bundle ‘core’, a three-helix bundle ‘arm’, and a C-terminal transmembrane (TM) helix. The PS2 core oligomerizes into hexameric units anchored in the mycomembrane by a channel-like coiled-coil of the TM helices. The PS2 arms mediate trimeric lattice contacts, crystallizing the hexameric units into an intricate semipermeable lattice. Using pulse-chase live cell imaging, we show that the PS2 lattice is incorporated at the poles, coincident with the actinobacterial elongasome. Finally, phylogenetic analysis shows a paraphyletic distribution and dispersed chromosomal location of PS2 in Corynebacteriales as a result of multiple recombination events and losses. These findings expand our understanding of S-layer biology and enable applications of membrane-supported self-assembling bioengineered materials.

show abstract

S-layer proteins as immune players: Tales from pathogenic and non-pathogenic bacteria

Cited by 3 publications

References 125 publications

The molecular architecture of Lactobacillus S-Layer: Assembly and attachment to teichoic acids

The molecular architecture of Lactobacillus S-Layer: Assembly and attachment to teichoic acids

S-layer proteins in microencapsulated freeze-dried probiotic Levilactobacillus brevis strains

Cryo-EM structure and polar assembly of the PS2 S-layer ofCorynebacterium glutamicum

Contact Info

Product

Resources

About