Bacterial cell-envelope glycoconjugates

Messner, Paul; Schäffer, Christina; Kosma, Paul

doi:10.1016/b978-0-12-408093-5.00006-x

Cited by 42 publications

(44 citation statements)

References 258 publications

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“…Hence, a more detailed and comprehensive summary cannot be given and is out of the scope of this review. Nevertheless, at this point, we would like to refer to several recent reviews providing deeper information on the glycosylation process in general (Albers & Meyer, ; Eichler & Maupin‐Furlow, ; Messner et al ., ).…”

Section: Isolation and Chemistrymentioning

confidence: 97%

“…(Stimson et al ., ).Thus, N‐glycosylation apparently is far more common in archaea than in bacteria. The degree of glycosylation of bacterial S‐layer proteins, that is, the covalent O‐glycosidic linkage of glycan moieties to select serine, threonine, and tyrosine residues, varies generally between 2% and 10% (w/w), and the S‐layer proteins are typically multiple glycosylated (Messner et al ., , ).…”

Section: Isolation and Chemistrymentioning

confidence: 99%

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S-layers: principles and applications

et al. 2014

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Monomolecular arrays of protein or glycoprotein subunits forming surface layers (S-layers) are one of the most commonly observed prokaryotic cell envelope components. S-layers are generally the most abundantly expressed proteins, have been observed in species of nearly every taxonomical group of walled bacteria, and represent an almost universal feature of archaeal envelopes. The isoporous lattices completely covering the cell surface provide organisms with various selection advantages including functioning as protective coats, molecular sieves and ion traps, as structures involved in surface recognition and cell adhesion, and as antifouling layers. S-layers are also identified to contribute to virulence when present as a structural component of pathogens. In Archaea, most of which possess S-layers as exclusive wall component, they are involved in determining cell shape and cell division. Studies on structure, chemistry, genetics, assembly, function, and evolutionary relationship of S-layers revealed considerable application potential in (nano)biotechnology, biomimetics, biomedicine, and synthetic biology.

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Section: Isolation and Chemistrymentioning

confidence: 97%

Section: Isolation and Chemistrymentioning

confidence: 99%

S-layers: principles and applications

et al. 2014

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“…Deaths from drug-resistant microbial infections are increasing(1, 2), approvals of new antibiotic classes are falling(1, 2), and there are increasing concerns about engineered biothreat agents that may be difficult to treat with conventional therapeutics (3). While broad spectrum infection vaccines potentially could be used to confront challenges relating to the increase in drug-resistant bacterial infections and decrease in approvals of new antibiotics, the major antigens on bacterial cell wall surfaces are poorly immunogenic, serotype-specific polysaccharides that do not easily support vaccine production (4,5). Some bacterial vaccines have been developed utilizing live attenuated bacteria (e.g.…”

Section: Introductionmentioning

confidence: 99%

Modular biomaterials vaccine technology protects against multiple pathogens and septic shock

Super

Doherty²,

Cartwright³

et al. 2020

Preprint

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Broad spectrum vaccines could provide a solution to the emergence of antibiotic resistant microbes, pandemics and engineered biothreat agents. Here, we describe a modular vaccine (composite infection vaccine technology (ciVAX)) which can be rapidly assembled and in which 4 of the 5 components are already approved for human use. ciVAX consists of an injectable biomaterial scaffold with factors to recruit and activate dendritic cells (DC) in vivo and microbeads conjugated with the broadspectrum opsonin Fc-Mannose-binding Lectin (FcMBL) that is pre-bound to polysaccharide-rich cell wall antigens, such as the pathogen-associated molecular patterns (PAMPs) fractions, captured from whole inactivated bacteria. Vaccination of mice and rabbits with ciVAX generates potent humoral and T cell responses to PAMPs isolated from native antibiotic-resistant E. coli and S. aureus, and ciVAX protects mice and pigs against lethal E coli challenge in sepsis and septic shock models. In addition to the efficacy of ciVAX against homologous challenge, PAMPS isolated from an infected animal protects other animals against infection by heterologous challenge using different E. coli serotypes -demonstrating the potential for use of ciVAX in controlling pandemics. The advantage of the ciVAX technology is the strong immunogenicity with limited reactogenicity, the use of inactivated pathogens, and the modular manufacture using cGMP approved products which can be stockpiled ready for the next pandemic.

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“…Chemical and genetically analysis of many S-layers has revealed a similar overall composition [4]. They are generally composed of a single protein or glycoprotein species with molecular masses ranging from 40 to 170 kDa [5].…”

Section: Introductionmentioning

confidence: 99%

Bioinformatic Survey of S-Layer Proteins in Bifidobacteria

Li¹,

Shen²,

Jiang³

et al. 2018

CMB

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Surface layer (S-layer) proteins are one of the most commonly observed cell envelope components in both Archaea and Bacteria. It has versatile functions and holds considerable application potential in biotechnology. Bifidobacteria are representative probiotics conferring health promoting properties. However, there is little study of S-layer in bifidobacteria yet. The distribution and characteristics of S-layer in bifidobacteria are unknown. In this study, search for S-layer protein in the identical protein groups in NCBI yielded 49 hits belonging to bifidobacteria. These proteins were annotated as either "S-layer (domain) protein" or "putative S-layer (y) domain protein" that distributed among 26 species of Bifidobacterium genus. Multiple alignments suggest S-layer proteins are relatively conservative. Phylogenetic analysis of 24 S-layer (domain) protein sequences groups them into three distinct clusters, with the majority species in Cluster-2. S-layer (domain) protein has a universe motif DUF4381, though its function is unknown. Meanwhile, two other motifs CARDB and EphA2_TM involved in cell adhesion and cell signaling respectively, presented in most S-layer (domain) protein in bifidobacteria. All S-layer proteins have a typical N-terminal Sec-dependent signal peptide and a C-terminal trans-membrane region. Homological modeling of representative S-layer proteins from each cluster revealed a few unique structural features. All representative S-layer proteins have a plenty of β-meander motif that exclusively composed by β-barrel structural architectures linked together by hairpin loops.

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Bacterial cell-envelope glycoconjugates

Cited by 42 publications

References 258 publications

S-layers: principles and applications

S-layers: principles and applications

Modular biomaterials vaccine technology protects against multiple pathogens and septic shock

Bioinformatic Survey of S-Layer Proteins in Bifidobacteria

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