Identification of the three-dimensional thioredoxin motif: related structure in the ORF3 protein of the Staphylococcus aureus mer operon

Biochemistry ◽  
1992 ◽  
Vol 31 (20) ◽  
pp. 4882-4891 ◽  
Author(s):  
Lynda B. M. Ellis ◽  
Peter Saurugger ◽  
Clare Woodward
Keyword(s):  
Staphylococcus Aureus ◽  
Three Dimensional ◽  
Related Structure ◽  
Mer Operon ◽  
Orf3 Protein

Three-dimensional origami paper-based device for portable immunoassay applications

Lab on a Chip ◽  
2019 ◽  
Vol 19 (4) ◽  
pp. 598-607 ◽  
Author(s):  
Chung-An Chen ◽  
Wen-Shin Yeh ◽  
Tsung-Ting Tsai ◽  
Yu-De Li ◽  
Chien-Fu Chen
Keyword(s):  
Staphylococcus Aureus ◽  
Synovial Fluid ◽  
Three Dimensional ◽  
Surface Modified ◽  
Human Synovial Fluid ◽  
Dimensional Surface ◽  
Analytical Device

A three-dimensional surface-modified origami-paper-based analytical device for Staphylococcus aureus detection in highly viscous human synovial fluid.

scholarly journals Three-Dimensional In Vitro Staphylococcus aureus Abscess Communities Display Antibiotic Tolerance and Protection from Neutrophil Clearance

2020 ◽  
Vol 88 (11) ◽  
Author(s):  
Marloes I. Hofstee ◽  
Martijn Riool ◽  
Igors Terjajevs ◽  
Keith Thompson ◽  
Martin J. Stoddart ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Immune Cells ◽  
Early Stage ◽  
Three Dimensional ◽  
Collagen Gel ◽  
Maximum Size ◽  
Human Neutrophils ◽  
Content Type

ABSTRACT Staphylococcus aureus is a prominent human pathogen in bone and soft-tissue infections. Pathophysiology involves abscess formation, which consists of central staphylococcal abscess communities (SACs), surrounded by a fibrin pseudocapsule and infiltrating immune cells. Protection against the ingress of immune cells such as neutrophils, or tolerance to antibiotics, remains largely unknown for SACs and is limited by the lack of availability of in vitro models. We describe a three-dimensional in vitro model of SACs grown in a human plasma-supplemented collagen gel. The in vitro SACs reached their maximum size by 24 h and elaborated a fibrin pseudocapsule, as confirmed by electron and immunofluorescence microscopy. The in vitro SACs tolerated 100× the MIC of gentamicin alone and in combination with rifampin, while planktonic controls and mechanically dispersed SACs were efficiently killed. To simulate a host response, SACs were exposed to differentiated PLB-985 neutrophil-like (dPLB) cells and to primary human neutrophils at an early stage of SAC formation or after maturation at 24 h. Both cell types were unable to clear mature in vitro SACs, but dPLB cells prevented SAC growth upon early exposure before pseudocapsule maturation. Neutrophil exposure after plasmin pretreatment of the SACs resulted in a significant decrease in the number of bacteria within the SACs. The in vitro SAC model mimics key in vivo features, offers a new tool to study host-pathogen interactions and drug efficacy assessment, and has revealed the functionality of the S. aureus pseudocapsule in protecting the bacteria from host phagocytic responses and antibiotics.

Deletion mutant analysis of the Staphylococcus aureus plasmid pI258 mercury-resistance determinant

1991 ◽  
Vol 37 (8) ◽  
pp. 624-631 ◽  
Author(s):  
Kenneth Babich ◽  
Mike Engle ◽  
Jeffery S. Skinner ◽  
Richard A. Laddaga
Keyword(s):  
Staphylococcus Aureus ◽  
Ion Transport ◽  
Copy Number ◽  
Deletion Mutant ◽  
Resistance Determinant ◽  
Mercury Resistance ◽  
Mutant Analysis ◽  
Mer Operon ◽  
Copy Number Plasmid ◽  
High Copy Number Plasmid

Deletion mutant analysis of the mercury-resistant determinant (mer operon) from the Staphylococcus aureus plasmid pI258 was used to verify the location of the merA and merB genes and to show the existence of mercuric ion transport gene(s). ORF5 was confirmed to be a transport gene and has an amino acid product sequence homologous to the merT gene products from several gram-negative bacteria and a Bacillus species. Deletion analysis established that inactivation of merA on a broad-spectrum mer resistance determinant resulted in a mercury-hypersensitive phenotype. Gene dosage had no apparent effect on the level of resistance conferred by the intact mer operon or on the expression of an inducible phenotype, except that when the intact pI258 mer operon was on a high copy number plasmid, uninduced cells possessed a volatilization rate that was at most only 3.5-fold less than that observed for induced cells. There was no need for mercury ion transport proteins for full resistance when the mer operon was expressed in a high copy number plasmid. Key words: mercury resistance, Staphylococcus aureus plasmid.

scholarly journals Identification ofypqPas a New Bacillus subtilis Biofilm Determinant That Mediates the Protection of Staphylococcus aureus against Antimicrobial Agents in Mixed-Species Communities

2014 ◽  
Vol 81 (1) ◽  
pp. 109-118 ◽  
Author(s):  
Pilar Sanchez-Vizuete ◽  
Dominique Le Coq ◽  
Arnaud Bridier ◽  
Jean-Marie Herry ◽  
Stéphane Aymerich ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Bacillus Subtilis ◽  
Extracellular Polymeric Substances ◽  
Antimicrobial Agents ◽  
Three Dimensional ◽  
Laboratory Strain ◽  
Spatial Arrangement ◽  
Content Type ◽  
Microbial Life ◽  
Multispecies Biofilms

ABSTRACTIn most habitats, microbial life is organized in biofilms, three-dimensional edifices sustained by extracellular polymeric substances that enable bacteria to resist harsh and changing environments. Under multispecies conditions, bacteria can benefit from the polymers produced by other species (“public goods”), thus improving their survival under toxic conditions. A recent study showed that aBacillus subtilishospital isolate (NDmed) was able to protectStaphylococcus aureusfrom biocide action in multispecies biofilms. In this work, we identifiedypqP, a gene whose product is required in NDmed for thick-biofilm formation on submerged surfaces and for resistance to two biocides widely used in hospitals. NDmed andS. aureusformed mixed biofilms, and both their spatial arrangement and pathogen protection were mediated by YpqP. FunctionalypqPis present in other naturalB. subtilisbiofilm-forming isolates. However, the gene is disrupted by the SPβ prophage in the weak submerged-biofilm-forming strains NCIB3610 and 168, which are both less resistant than NDmed to the biocides tested. Furthermore, in a 168 laboratory strain cured of the SPβ prophage, the reestablishment of a functionalypqPgene led to increased thickness and resistance to biocides of the associated biofilms. We therefore propose that YpqP is a new and important determinant ofB. subtilissurface biofilm architecture, protection against exposure to toxic compounds, and social behavior in bacterial communities.

Synthesis, crystal structure, and magnetic properties of a multicage compound: [(Me)2EtNH][Mn(N3)3] with a perovskite-related structure

2019 ◽  
Vol 74 (4) ◽  
pp. 335-339 ◽  
Author(s):  
Jie Yang ◽  
Yuan Huang ◽  
Ting Fang ◽  
Kun Qian ◽  
Wen-Bin Chen ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Second Harmonic Generation ◽  
Harmonic Generation ◽  
Magnetic Measurements ◽  
Second Harmonic ◽  
Three Dimensional ◽  
Related Structure ◽  
X Ray Diffraction ◽  
X Ray ◽  
Polar Crystal

AbstractA new multicage compound [(Me)2EtNH][Mn(N3)3] (Me = methyl, Et = ethyl) with a perovskite-related structure has been synthesized. The manganese(II) cations are bridged by end-to-end (EE) azide anions to form three-dimensional cages with the N,N-dimethylethylammonium cations residing in the cavities of the [Mn(N3)3]nn− cages. The compound has been characterized by single-crystal X-ray diffraction, IR spectroscopy, elemental analysis, second-harmonic generation, and magnetic measurements. The second-harmonic generation results support its noncentrosymmetric polar crystal structure. Magnetic susceptibility measurements show antiferromagnetic interactions among the MnII ions.

scholarly journals Identification and “in silico” Structural Analysis of the Glutamine-rich Protein Qrp (YheA) in Staphylococcus Aureus

2019 ◽  
Vol 12 (1) ◽  
pp. 18-29
Author(s):  
Javier Escobar-Perez ◽  
Katterine Ospina-Garcia ◽  
Zayda Lorena Corredor Rozo ◽  
Ricaurte Alejandro Marquez-Ortiz ◽  
Jaime E Castellanos ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Structural Analysis ◽  
Protein Function ◽  
In Silico ◽  
3D Structure ◽  
Three Dimensional ◽  
3D Models ◽  
Protein Domain ◽  
Dimensional Structure ◽  
Biofilm Growth

Background: YlbF and YmcA are two essential proteins for the formation of biofilm, sporulation, and competence in Bacillus subtilis. In these two proteins, a new protein domain called com_ylbF was recently discovered, but its role and protein function has not yet been established. Objective: In this study, we identified and performed an “in silico” structural analysis of the YheA protein, another com_ylbF-containing protein, in the opportunistic pathogen Staphylococcus aureus. Methods: The search of the yheA gene was performed using BLAST-P and tBLASn algorithms. The three-dimensional (3D) models of YheA, as well as YlbF and YmcA proteins, were built using the I-TASSER and Quark programs. The identification of the native YheA in Staphylococcus aureus was carried out through chromatography using the FPLC system. Results: We found that YheA protein is more widely distributed in Gram-positive bacteria than YlbF and YmcA. Two new and important characteristics for YheA and other com_ylbF-containing proteins were found: a highly conserved 3D structure and the presence of a putative conserved motif located in the central region of the domain, which could be involved in its function. Additionally, we established that Staphylococcus aureus expresses YheA protein in both planktonic growth and biofilm. Finally, we suggest renaming YheA as glutamine-rich protein (Qrp) in S. aureus. Conclusion: The Grp (YheA), YlbF, and YmcA proteins adopt a highly conserved three-dimensional structure, harboring a protein-specific putative motif within the com_ylbF domain, which possibly favors the interaction with their substrates. Finally, Staphylococcus aureus expresses the Grp (YheA) protein in both planktonic and biofilm growth.

scholarly journals Three-dimensional structures of Lipoproteins from Streptococcus pneumoniae and Staphylococcus aureus

2018 ◽  
Vol 308 (6) ◽  
pp. 692-704 ◽  
Author(s):  
Sergio G. Bartual ◽  
Martín Alcorlo ◽  
Siseth Martínez-Caballero ◽  
Rafael Molina ◽  
Juan A. Hermoso
Keyword(s):  
Staphylococcus Aureus ◽  
Streptococcus Pneumoniae ◽  
Three Dimensional ◽  
And Staphylococcus Aureus

scholarly journals Unbiased Identification of Immunogenic Staphylococcus aureus Leukotoxin B-Cell Epitopes

2020 ◽  
Vol 88 (4) ◽  
Author(s):  
David N. Hernandez ◽  
Kayan Tam ◽  
Bo Shopsin ◽  
Emily E. Radke ◽  
Pegah Kolahi ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Phage Display ◽  
B Cell ◽  
Three Dimensional ◽  
Amino Acid Side Chain ◽  
Gene Fragment ◽  
B Cell Epitopes ◽  
Content Type ◽  
Amino Acid Peptide

ABSTRACT Unbiased identification of individual immunogenic B-cell epitopes in major antigens of a pathogen remains a technology challenge for vaccine discovery. We therefore developed a platform for rapid phage display screening of deep recombinant libraries consisting of as few as one major pathogen antigen. Using the bicomponent pore-forming leukocidin (Luk) exotoxins of the major pathogen Staphylococcus aureus as a prototype, we randomly fragmented and separately ligated the hemolysin gamma A (HlgA) and LukS genes into a custom-built phage display system, termed pComb-Opti8. Deep sequence analysis of barcoded amplimers of the HlgA and LukS gene fragment libraries demonstrated that biopannng against a cross-reactive anti-Luk monoclonal antibody (MAb) recovered convergent molecular clones with short overlapping homologous sequences. We thereby identified an 11-amino-acid sequence that is highly conserved in four Luk toxin subunits and is ubiquitous in representation within S. aureus clinical isolates. The isolated 11-amino-acid peptide probe was predicted to retain the native three-dimensional (3D) conformation seen within the Luk holotoxin. Indeed, this peptide was recognized by the selecting anti-Luk MAb, and, using mutated peptides, we showed that a particular amino acid side chain was essential for these interactions. Furthermore, murine immunization with this peptide elicited IgG responses that were highly reactive with both the autologous synthetic peptide and the full-length Luk toxin homologues. Thus, using a gene fragment- and phage display-based pipeline, we have identified and validated immunogenic B-cell epitopes that are cross-reactive between members of the pore-forming leukocidin family. This approach could be harnessed to identify novel epitopes for a much-needed S. aureus-protective subunit vaccine.

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