Skip to content
Review

Forming Strong Bonds: Building Microbial Surface Structures by Donor-Strand Exchange.

Jul 2026 · Annual Review of Microbiology · 0 citations
Medicine

TL;DR

This review focuses on bacterial and archaeal systems that utilize donor-strand exchange (DSE) interactions between subunit proteins, highlighting how DSE-mediated polymerization contributes to the assembly of extracellular structures in both the bacterial and archaeal domains.

Abstract

Microbial organisms assemble a diverse array of surface structures to facilitate critical functions including motility, adhesion, and biofilm formation. As extracellular organelles, pili and related surface structures must be able to function in harsh environments and withstand various stressors. Microbes have evolved different strategies to assemble structures able to function under these challenging conditions. This review focuses on bacterial and archaeal systems that utilize donor-strand exchange (DSE) interactions between subunit proteins. DSE is a noncovalent assembly mechanism where one subunit contributes a β-strand to complete the structure of its neighboring subunit. This subunit-subunit interaction is one of the strongest noncovalent interactions known, with the resulting fiber being capable of withstanding extreme environmental stresses and shear forces. We summarize the structural biology and biogenesis of these surface structures, highlighting how DSE-mediated polymerization contributes to the assembly of extracellular structures in both the bacterial and archaeal domains.

View source

Similar papers

Review Open access Aug 2026

Structural diversity and functional versatility in Gram-positive S-layers.

This review addresses S-layer structure and function in Gram-positive bacteria, with emphasis on emerging insights into lattice-forming self-assembly and the mechanisms by which S-layers attach to the cell wall.

A. Sogues, Han K. Remaut · 0 citations
Open access Aug 2026

Structure of a key adhesin-exopolysaccharide interaction provides insights into matrix assembly in Vibrio cholerae biofilms

The structure reveals for the first time the interaction between a biofilm exopolysaccharide and matrix protein, as well as insights into conformational changes of exopolysaccharide induced by this binding, and provides a generalizable approach for studying the biophysical and biochemical properties of carbohydrate-dep...

Alex Hinbest, Hyerim Bianca Nam, E. Liszczyk et al. · 0 citations
Open access Aug 2026

Self-assembly of surface layer protein SbsC from Geobacillus stearothermophilus and common principles of Bacilli S-layers

Given the involvement of S-layers in host interactions, immune evasion, and pathogenicity, particularly in Bacillusanthracis and Bacillus cereus group species, the identified intermolecular interfaces represent attractive targets for the development of novel antibacterial strategies.

Christoph Grininger, L. Gambelli, Anđela Ðordić et al. · 0 citations
#protein folding Open access Aug 2026

Three hydrophobic surface binding a proteins link surface hydrophobicity to sporulation, biofilm formation, and host interaction in Mucor lusitanicus

Results show that HsbA proteins in Mucor lusitanicus function as regulators that couple fungal surface remodeling with developmental transitions, thereby coordinating environmental adaptation and host–pathogen interactions.

Anna Molnár, Amanda Grace Vaz, M. Homa et al. · 0 citations
#protein folding Open access Sep 2026

Protein architectures of the bacterial spore envelope - common principles of assembly

These findings provide the first molecular framework for understanding the organisation and assembly of the Clostridium spore envelope and reveal previously unrecognised principles governing the evolution of protective proteinaceous structures across the Bacillota (Firmicutes).

Hannah Fisher, Abigail R. E. Roberts, Ainhoa Dafis-Sagarmendi et al. · 0 citations

We use cookies to run the site and, with your consent, for analytics and to show ads. See our Cookie Policy.