scholarly journals S-layers: The Proteinaceous Multifunctional Armors of Gram-Positive Pathogens

2021 ◽  
Vol 12 ◽  
Author(s):  
Janani Ravi ◽  
Antonella Fioravanti
Keyword(s):  
Layer Structure ◽  
Cell Envelope ◽  
Sequence Structure ◽  
Gram Positive ◽  
Host Interactions ◽  
Clostridioides Difficile ◽  
Associated Proteins ◽  
Experimental Findings ◽  
Cell Envelopes ◽  
And Function

S-layers are self-assembled crystalline 2D lattices enclosing the cell envelopes of several bacteria and archaea. Despite their abundance, the landscape of S-layer structure and function remains a land of wonder. By virtue of their location, bacterial S-layers have been hypothesized to add structural stability to the cell envelope. In addition, S-layers are implicated in mediating cell-environment and cell-host interactions playing a key role in adhesion, cell growth, and division. Significant strides in the understanding of these bacterial cell envelope components were made possible by recent studies that have provided structural and functional insights on the critical S-layer and S-layer-associated proteins (SLPs and SLAPs), highlighting their roles in pathogenicity and their potential as therapeutic or vaccine targets. In this mini-review, we revisit the sequence-structure-function relationships of S-layers, SLPs, and SLAPs in Gram-positive pathogens, focusing on the best-studied classes, Bacilli (Bacillus anthracis) and Clostridia (Clostridioides difficile). We delineate the domains and their architectures in archetypal S-layer proteins across Gram-positive genera and reconcile them with experimental findings. Similarly, we highlight a few key “flavors” of SLPs displayed by Gram-positive pathogens to assemble and support the bacterial S-layers. Together, these findings indicate that S-layers are excellent candidates for translational research (developing diagnostics, antibacterial therapeutics, and vaccines) since they display the three crucial characteristics: accessible location at the cell surface, abundance, and unique lineage-specific signatures.

scholarly journals Macroamphiphilic Components of Thermophilic Actinomycetes: Identification of Lipoteichoic Acid in Thermobifida fusca

2008 ◽  
Vol 191 (1) ◽  
pp. 152-160 ◽  
Author(s):  
Obaidur Rahman ◽  
Markus Pfitzenmaier ◽  
Oxana Pester ◽  
Siegfried Morath ◽  
Stephen P. Cummings ◽  
...  
Keyword(s):  
Cell Envelope ◽  
Teichoic Acid ◽  
Lipoteichoic Acid ◽  
Thermobifida Fusca ◽  
Membrane Composition ◽  
Gram Positive ◽  
Thermophilic Actinomycetes ◽  
Gram Positive Bacteria ◽  
Cell Envelopes ◽  
Lipoteichoic Acids

ABSTRACT The cell envelopes of gram-positive bacteria contain structurally diverse membrane-anchored macroamphiphiles (lipoteichoic acids and lipoglycans) whose functions are poorly understood. Since regulation of membrane composition is an important feature of adaptation to life at higher temperatures, we have examined the nature of the macroamphiphiles present in the thermophilic actinomycetes Thermobifida fusca and Rubrobacter xylanophilus. Following hot-phenol-water extraction and purification by hydrophobic interaction chromatography, Western blotting with a monoclonal antibody against lipoteichoic acid strongly suggested the presence of a polyglycerophosphate lipoteichoic acid in T. fusca. This structure was confirmed by chemical and nuclear magnetic resonance analyses, which confirmed that the lipoteichoic acid is substituted with β-glucosyl residues, in common with the teichoic acid of this organism. In contrast, several extraction methods failed to recover significant macroamphiphilic carbohydrate- or phosphate-containing material from R. xylanophilus, suggesting that this actinomycete most likely lacks a membrane-anchored macroamphiphile. The finding of a polyglycerophosphate lipoteichoic acid in T. fusca suggests that lipoteichoic acids may be more widely present in the cell envelopes of actinomycetes than was previously assumed. However, the apparent absence of macroamphiphiles in the cell envelope of R. xylanophilus is highly unusual and suggests that macroamphiphiles may not always be essential for cell envelope homeostasis in gram-positive bacteria.

Structure, Biosynthesis, and Function of Teichoic Acids and Related Cell Wall Glycopolymers in the Gram-positive Cell Envelope

2010 ◽  
pp. 155-174 ◽  
Author(s):  
Maren Rautenberg ◽  
Thomas Kohler ◽  
Guoqing Xia ◽  
Emir Kulauzovic ◽  
Andreas Peschel
Keyword(s):  
Cell Wall ◽  
Cell Envelope ◽  
Gram Positive ◽  
Teichoic Acids ◽  
Related Cell ◽  
And Function

scholarly journals In Situ Characterization of Differences in the Viscoelastic Response of Individual Gram-Negative and Gram-Positive Bacterial Cells

2009 ◽  
Vol 191 (17) ◽  
pp. 5518-5525 ◽  
Author(s):  
Virginia Vadillo-Rodriguez ◽  
Sarah R. Schooling ◽  
John R. Dutcher
Keyword(s):  
Viscoelastic Properties ◽  
Cell Envelope ◽  
Outer Membrane Proteins ◽  
Elastic Response ◽  
Bacterial Cells ◽  
Structure Property ◽  
Gram Positive ◽  
Gram Negative ◽  
Structure Property Relationships ◽  
Cell Envelopes

ABSTRACT We used a novel atomic force microscopy (AFM)-based technique to compare the local viscoelastic properties of individual gram-negative (Escherichia coli) and gram-positive (Bacillus subtilis) bacterial cells. We found that the viscoelastic properties of the bacterial cells are well described by a three-component mechanical model that combines an instantaneous elastic response and a delayed elastic response. These experiments have allowed us to investigate the relationship between the viscoelastic properties and the structure and composition of the cell envelope. In addition, this is the first report in which the mechanical role of Lpp, the major peptidoglycan-associated lipoprotein and one of the most abundant outer membrane proteins in E. coli cells, has been quantified. We expect that our findings will be helpful in increasing the understanding of the structure-property relationships of bacterial cell envelopes.

Molecular architecture and functions of the neuronal cytoskeleton

1990 ◽  
Vol 48 (3) ◽  
pp. 2-3
Author(s):  
Nobutaka Hirokawa
Keyword(s):  
Major Elements ◽  
Molecular Structures ◽  
Organelle Transport ◽  
Molecular Architecture ◽  
Neuronal Morphogenesis ◽  
Microtubule Associated Proteins ◽  
Associated Proteins ◽  
And Function ◽  
Small Clusters

In this symposium I will present our studies about the molecular architecture and function of the cytomatrix of the nerve cells. The nerve cell is a highly polarized cell composed of highly branched dendrites, cell body, and a single long axon along the direction of the impulse propagation. Each part of the neuron takes characteristic shapes for which the cytoskeleton provides the framework. The neuronal cytoskeletons play important roles on neuronal morphogenesis, organelle transport and the synaptic transmission. In the axon neurofilaments (NF) form dense arrays, while microtubules (MT) are arranged as small clusters among the NFs. On the other hand, MTs are distributed uniformly, whereas NFs tend to run solitarily or form small fascicles in the dendrites Quick freeze deep etch electron microscopy revealed various kinds of strands among MTs, NFs and membranous organelles (MO). These structures form major elements of the cytomatrix in the neuron. To investigate molecular nature and function of these filaments first we studied molecular structures of microtubule associated proteins (MAP1A, MAP1B, MAP2, MAP2C and tau), and microtubules reconstituted from MAPs and tubulin in vitro. These MAPs were all fibrous molecules with different length and formed arm like projections from the microtubule surface.

scholarly journals Significance of Mast Cell Formed Extracellular Traps in Microbial Defense

2021 ◽  
Author(s):  
Daniel Elieh Ali Komi ◽  
Wolfgang M. Kuebler
Keyword(s):  
State Of The Art ◽  
Extracellular Dna ◽  
Cellular Mechanisms ◽  
Extracellular Traps ◽  
Synthetic Chemicals ◽  
Dna Strands ◽  
Associated Proteins ◽  
Microbial Defense ◽  
And Function ◽  
Insight Into

AbstractMast cells (MCs) are critically involved in microbial defense by releasing antimicrobial peptides (such as cathelicidin LL-37 and defensins) and phagocytosis of microbes. In past years, it has become evident that in addition MCs may eliminate invading pathogens by ejection of web-like structures of DNA strands embedded with proteins known together as extracellular traps (ETs). Upon stimulation of resting MCs with various microorganisms, their products (including superantigens and toxins), or synthetic chemicals, MCs become activated and enter into a multistage process that includes disintegration of the nuclear membrane, release of chromatin into the cytoplasm, adhesion of cytoplasmic granules on the emerging DNA web, and ejection of the complex into the extracellular space. This so-called ETosis is often associated with cell death of the producing MC, and the type of stimulus potentially determines the ratio of surviving vs. killed MCs. Comparison of different microorganisms with specific elimination characteristics such as S pyogenes (eliminated by MCs only through extracellular mechanisms), S aureus (removed by phagocytosis), fungi, and parasites has revealed important aspects of MC extracellular trap (MCET) biology. Molecular studies identified that the formation of MCET depends on NADPH oxidase-generated reactive oxygen species (ROS). In this review, we summarize the present state-of-the-art on the biological relevance of MCETosis, and its underlying molecular and cellular mechanisms. We also provide an overview over the techniques used to study the structure and function of MCETs, including electron microscopy and fluorescence microscopy using specific monoclonal antibodies (mAbs) to detect MCET-associated proteins such as tryptase and histones, and cell-impermeant DNA dyes for labeling of extracellular DNA. Comparing the type and biofunction of further MCET decorating proteins with ETs produced by other immune cells may help provide a better insight into MCET biology in the pathogenesis of autoimmune and inflammatory disorders as well as microbial defense.

scholarly journals Membrane-associated phase separation: organization and function emerge from a two-dimensional milieu

2021 ◽  
Author(s):  
Jonathon A Ditlev
Keyword(s):  
Phase Separation ◽  
Cell Biology ◽  
Cellular Environment ◽  
Condensate Formation ◽  
Associated Proteins ◽  
Available Technology ◽  
And Function ◽  
Surrounding Membrane

Abstract Liquid‒liquid phase separation (LLPS) of biomolecules has emerged as an important mechanism that contributes to cellular organization. Phase separated biomolecular condensates, or membrane-less organelles, are compartments composed of specific biomolecules without a surrounding membrane in the nucleus and cytoplasm. LLPS also occurs at membranes, where both lipids and membrane-associated proteins can de-mix to form phase separated compartments. Investigation of these membrane-associated condensates using in vitro biochemical reconstitution and cell biology has provided key insights into the role of phase separation in membrane domain formation and function. However, these studies have generally been limited by available technology to study LLPS on model membranes and the complex cellular environment that regulates condensate formation, composition, and function. Here, I briefly review our current understanding of membrane-associated condensates, establish why LLPS can be advantageous for certain membrane-associated condensates, and offer a perspective for how these condensates may be studied in the future.

scholarly journals riboCIRC: a comprehensive database of translatable circRNAs

2021 ◽  
Vol 22 (1) ◽  
Author(s):  
Huihui Li ◽  
Mingzhe Xie ◽  
Yan Wang ◽  
Ludong Yang ◽  
Zhi Xie ◽  
...  
Keyword(s):  
De Novo ◽  
Species Conservation ◽  
Structure And Function ◽  
Research Community ◽  
Genome Browser ◽  
Valuable Resource ◽  
Sequence Structure ◽  
A Genome ◽  
Context Specific ◽  
And Function

AbstractriboCIRC is a translatome data-oriented circRNA database specifically designed for hosting, exploring, analyzing, and visualizing translatable circRNAs from multi-species. The database provides a comprehensive repository of computationally predicted ribosome-associated circRNAs; a manually curated collection of experimentally verified translated circRNAs; an evaluation of cross-species conservation of translatable circRNAs; a systematic de novo annotation of putative circRNA-encoded peptides, including sequence, structure, and function; and a genome browser to visualize the context-specific occupant footprints of circRNAs. It represents a valuable resource for the circRNA research community and is publicly available at http://www.ribocirc.com.

Structure and function of seed lipid body-associated proteins

2008 ◽  
Vol 331 (10) ◽  
pp. 746-754 ◽  
Author(s):  
Zita Purkrtova ◽  
Pascale Jolivet ◽  
Martine Miquel ◽  
Thierry Chardot
Keyword(s):  
Lipid Body ◽  
Structure And Function ◽  
Seed Lipid ◽  
Associated Proteins ◽  
And Function

scholarly journals N 1 N 8-bis(γ-glutamyl)spermidine cross-linking in epidermal-cell envelopes. Comparison of cross-link levels in normal and psoriatic cell envelopes

1990 ◽  
Vol 271 (2) ◽  
pp. 305-308 ◽  
Author(s):  
N Martinet ◽  
S Beninati ◽  
T P Nigra ◽  
J E Folk
Keyword(s):  
Epidermal Cell ◽  
Skin Disease ◽  
Envelope Protein ◽  
Cell Envelope ◽  
Human Epidermis ◽  
Cross Linking ◽  
Cross Link ◽  
Gamma Glutamyl ◽  
Cell Envelopes ◽  
Isolated Cell

N1N8-Bis(gamma-glutamyl)spermidine was found in exhaustive proteolytic digests of isolated cell envelopes from human epidermis at levels comparable with those of epsilon-(gamma-glutamyl)lysine. Significantly higher than normal amounts of these compounds, particularly the bis(gamma-glutamyl)polyamine, were observed in envelopes from afflicted areas (scales) of psoriatic patients. These findings support the notions that N1N8-bis(gamma-glutamyl)spermidine, like epsilon-(gamma-glutamyl)lysine, functions in cell envelopes as an enzyme-generated protein cross-link and stabilizing force and that individuals with the chronic, recurrent skin disease, psoriasis, exhibit in involved epidermis abnormal cell-envelope-protein cross-linking.

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