Streptococcal M Protein: A Common Structural Motif Used by Gram-Positive Bacteria for Biologically Active Surface Molecules

1992 ◽  
pp. 31-38 ◽  
Author(s):  
V. A. Fischetti ◽  
V. Pancholi ◽  
P. Sellers ◽  
J. Schmidt ◽  
G. Landau ◽  
...  
Keyword(s):  
Protein A ◽  
Active Surface ◽  
Biologically Active ◽  
Structural Motif ◽  
M Protein ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Surface Molecules ◽  
Streptococcal M Protein

scholarly journals Identification of an endogenous membrane anchor-cleaving enzyme for group A streptococcal M protein. Its implication for the attachment of surface proteins in gram-positive bacteria.

1989 ◽  
Vol 170 (6) ◽  
pp. 2119-2133 ◽  
Author(s):  
V Pancholi ◽  
V A Fischetti
Keyword(s):  
Cell Wall ◽  
Sequence Similarity ◽  
Surface Proteins ◽  
M Protein ◽  
Membrane Anchor ◽  
Gram Positive ◽  
Streptococcal Cell Wall ◽  
Gram Positive Bacteria ◽  
Streptococcal M Protein ◽  
Triton X

How streptococcal M protein or other surface proteins of gram-positive bacteria are anchored to the cell is poorly understood. Previously, we reported that M protein released after cell wall removal with a muralytic enzyme lacked the COOH terminal hydrophobic amino acids and charged tail predicted from DNA sequence. An endogenous membrane anchor-cleaving enzyme has now been identified with the ability to release M protein from isolated streptococcal protoplasts. At pH 5.5 in the presence of 30% raffinose, the streptococcal cell wall may be removed with a muralytic enzyme without releasing M protein from the resulting protoplasts indicating that the M molecule is attached through the bacterial cytoplasmic membrane. Release of M molecules occurs when the M protein-charged protoplasts are placed in raffinose buffer at pH 7.4. Although Zn2+, Cd2+, Ca2+, PHMB, and pHMPS inhibit the activity of the releasing enzyme, the blocking activity of Zn2+, Cd2+, and Ca2+ are reversible while PHMB and pHMPS are irreversible. PHMB-treated protoplasts are unable to release M protein at pH 7.4. However, M protein is liberated from these protoplasts when mixed with those prepared from M- streptococci serving as an enzyme source. The supernatant from M- protoplasts is unable to release M protein from PHMB-inactivated M+ protoplasts, confirming that the anchor-cleaving enzyme is membrane bound. Thus, the M protein releasing activity appears to be the result of a thiol-dependent anchor-cleaving enzyme. Streptococcal membranes treated with sodium carbonate and Triton X-114 still retain the M protein verifying that it is an integral membrane molecule. Evidence also is presented indicating significant sequence similarity between M protein and certain GPI-anchored proteins in the region responsible for protein anchoring.

scholarly journals A Pilot Study of Bacteriological Population Changes through Potable Water Treatment and Distribution

2000 ◽  
Vol 66 (1) ◽  
pp. 268-276 ◽  
Author(s):  
Cheryl D. Norton ◽  
Mark W. LeChevallier
Keyword(s):  
Pilot Study ◽  
Biologically Active ◽  
Plate Count ◽  
Identification System ◽  
Population Changes ◽  
Gram Positive ◽  
Pipe Surface ◽  
Treated Water ◽  
Gram Positive Bacteria ◽  
Biofilm Development

ABSTRACT This pilot study compares the compositions of bacterial biofilms in pipe networks supplied with water containing either high levels of biodegradable organic matter (BOM) or low levels of BOM (conventionally or biologically treated, respectively). The Microbial Identification System for fatty acid analysis was utilized in this study to identify a large number of organisms (>1,400) to determine population changes in both conventionally and biologically treated water and biofilms. Data generated during this study indicated that suspended bacteria have little impact on biofilms, and despite treatment (conventional or biological), suspended microbial populations were similar following disinfection. Prechlorination with free chlorine resulted not only in reduced plate count values but also in a dramatic shift in the composition of the bacterial population to predominately gram-positive bacteria. Chlorination of biologically treated water produced the same shifts toward gram-positive bacteria. Removal of assimilable organic carbon by the biologically active filters slowed the rate of biofilm accumulation, but biofilm levels were similar to those found in conventionally treated water within several weeks. Iron pipes stimulated the rate of biofilm development, and bacterial levels on disinfected iron pipes exceeded those for chlorinated polyvinyl chloride pipes. The study showed that the iron pipe surface dramatically influenced the composition, activity, and disinfection resistance of biofilm bacteria.

scholarly journals Synthesis and Evaluation of Antimicrobial and Cytotoxic Activity of Oxathiine-Fused Quinone-Thioglucoside Conjugates of Substituted 1,4-Naphthoquinones

Molecules ◽  
2020 ◽  
Vol 25 (16) ◽  
pp. 3577
Author(s):  
Yuri E. Sabutski ◽  
Ekaterina S. Menchinskaya ◽  
Ludmila S. Shevchenko ◽  
Ekaterina A. Chingizova ◽  
Artur R. Chingizov ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Cytotoxic Activity ◽  
Antimicrobial Activities ◽  
Biologically Active ◽  
Hydroxyl Group ◽  
Diffusion Method ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
High Cytotoxic Activity ◽  
Derivatives Of

A series of new tetracyclic oxathiine-fused quinone-thioglycoside conjugates based on biologically active 1,4-naphthoquinones and 1-mercapto derivatives of per-O-acetyl d-glucose, d-galactose, d-xylose, and l-arabinose have been synthesized, characterized, and evaluated for their cytotoxic and antimicrobial activities. Six tetracyclic conjugates bearing a hydroxyl group in naphthoquinone core showed high cytotoxic activity with EC50 values in the range of 0.3 to 0.9 μM for various types of cancer and normal cells and no hemolytic activity up to 25 μM. The antimicrobial activity of conjugates was screened against Gram-positive bacteria (Staphylococcus aureus, Bacillus cereus), Gram-negative bacteria (Pseudomonas aeruginosa and Escherichia coli), and fungus Candida albicans by the agar diffusion method. The most effective juglone conjugates with d-xylose or l-arabinose moiety and hydroxyl group at C-7 position of naphthoquinone core at concentration 10 µg/well showed antimicrobial activity comparable with antibiotics vancomicin and gentamicin against Gram-positive bacteria strains. In liquid media, juglone-arabinosidic tetracycles showed highest activity with MIC 6.25 µM. Thus, a positive effect of heterocyclization with mercaptosugars on cytotoxic and antimicrobial activity for group of 1,4-naphthoquinones was shown.

scholarly journals Human C4b-binding Protein, Structural Basis for Interaction with Streptococcal M Protein, a Major Bacterial Virulence Factor

2005 ◽  
Vol 281 (6) ◽  
pp. 3690-3697 ◽  
Author(s):  
Huw T. Jenkins ◽  
Linda Mark ◽  
Graeme Ball ◽  
Jenny Persson ◽  
Gunnar Lindahl ◽  
...  
Keyword(s):  
Virulence Factor ◽  
Binding Protein ◽  
Protein A ◽  
Bacterial Virulence ◽  
M Protein ◽  
Structural Basis ◽  
Streptococcal M Protein ◽  
Bacterial Virulence Factor

scholarly journals Synthesis and Antimicrobial Activity of Burkholderia-Related 4-Hydroxy-3-Methyl-2-Alkenylquinolones (HMAQs) and Their N-Oxide Counterparts

2020 ◽  
Author(s):  
Marianne Piochon ◽  
Pauline M. L. Coulon ◽  
Armand Caulet ◽  
Marie-Christine Groleau ◽  
Eric Déziel ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Biologically Active ◽  
Specific Class ◽  
Gram Positive ◽  
Carbonate Group ◽  
Gram Positive Bacteria ◽  
Alkenyl Chain ◽  
Optimized Conditions ◽  
Burkholderia Ambifaria

ABSTRACT: The Burkholderia genus offers a promising potential in medicine because of the diversity of biologically active natural products encoded in its genome. Some pathogenic Burkholderia spp. biosynthesize a specific class of antimicrobial 2-alkyl-4(1H)-quinolones, i.e., 4-hydroxy-3-methyl-2-alkenylquinolones (HMAQs) and their N-oxide derivatives (HMAQNOs). Herein, we report the synthesis of a series of six HMAQs and HMAQNOs featuring a trans-∆<sup>2</sup> double bond at the C2-alkyl chain. The quinolone scaffold was obtained via the Conrad-Limpach approach while the (E)-2-alkenyl chain was inserted through Suzuki-Miyaura cross-coupling under microwave radiation without noticeable isomerization according to the optimized conditions. Subsequent oxidation of enolate-protected HMAQs cleanly led to the formation of HMAQNOs following cleavage of the ethyl carbonate group. Synthetic HMAQs and HMAQNOs were in vitro evaluated for their antimicrobial activity against different Gram-negative and Gram-positive bacteria as well as against fungi and yeasts. The biological results support and extend the potential of HMAQs and HMAQNOs as antimicrobials, especially against Gram-positive bacteria. We also confirm the involvement of HMAQs in the autoregulation of the Hmq system in Burkholderia ambifaria.

Biologically active binaphthol-scaffolded imidazolium salts

MedChemComm ◽  
2014 ◽  
Vol 5 (4) ◽  
pp. 436-440 ◽  
Author(s):  
Marc Vidal ◽  
Claude-Rosny Elie ◽  
Shirley Campbell ◽  
Audrey Claing ◽  
Andreea R. Schmitzer
Keyword(s):  
Antimicrobial Activity ◽  
Lipid Membrane ◽  
Biologically Active ◽  
Imidazolium Salts ◽  
Gram Positive ◽  
Gram Positive Bacteria

This work describes the antimicrobial activity and selectivity for Gram-positive bacteria of imidazolium-functionalized binols, as a result of their insertion into the lipid membrane and alteration of its permeability.

scholarly journals The Sortase SrtA of Listeria monocytogenes Is Involved in Processing of Internalin and in Virulence

2002 ◽  
Vol 70 (3) ◽  
pp. 1382-1390 ◽  
Author(s):  
Caroline Garandeau ◽  
Hélène Réglier-Poupet ◽  
Iharilalao Dubail ◽  
Jean-Luc Beretti ◽  
Patrick Berche ◽  
...  
Keyword(s):  
Cell Wall ◽  
Listeria Monocytogenes ◽  
Protein A ◽  
Knockout Mutant ◽  
Reporter Protein ◽  
Gram Positive ◽  
Bacterial Surface ◽  
Gram Positive Bacteria ◽  
Covalently Linked

ABSTRACT Listeria monocytogenes is an intracellular gram-positive human pathogen that invades eucaryotic cells. Among the surface-exposed proteins playing a role in this invasive process, internalin belongs to the family of LPXTG proteins, which are known to be covalently linked to the bacterial cell wall in gram-positive bacteria. Recently, it has been shown in Staphylococcus aureus that the covalent anchoring of protein A, a typical LPXTG protein, is due to a cysteine protease, named sortase, required for bacterial virulence. Here, we identified in silico from the genome of L. monocytogenes a gene, designated srtA, encoding a sortase homologue. The role of this previously unknown sortase was studied by constructing a sortase knockout mutant. Internalin was used as a reporter protein to study the effects of the srtA mutation on cell wall anchoring of this LPXTG protein in L. monocytogenes. We show that the srtA mutant (i) is affected in the display of internalin at the bacterial surface, (ii) is significantly less invasive in vitro, and (iii) is attenuated in its virulence in the mouse. These results demonstrate that srtA of L. monocytogenes acts as a sortase and plays a role in the pathogenicity.

scholarly journals The First Structure of a Lantibiotic Immunity Protein, SpaI from Bacillus subtilis, Reveals a Novel Fold

2012 ◽  
Vol 287 (42) ◽  
pp. 35286-35298 ◽  
Author(s):  
Nina A. Christ ◽  
Sophie Bochmann ◽  
Daniel Gottstein ◽  
Elke Duchardt-Ferner ◽  
Ute A. Hellmich ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Lipid Membranes ◽  
Biologically Active ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Lipid Ii ◽  
Terminal Fragment ◽  
Terminal Amino ◽  
Immunity Mechanism ◽  
Producer Strains

Lantibiotics are peptide-derived antibiotics that inhibit the growth of Gram-positive bacteria via interactions with lipid II and lipid II-dependent pore formation in the bacterial membrane. Due to their general mode of action the Gram-positive producer strains need to express immunity proteins (LanI proteins) for protection against their own lantibiotics. Little is known about the immunity mechanism protecting the producer strain against its own lantibiotic on the molecular level. So far, no structures have been reported for any LanI protein. We solved the structure of SpaI, a LanI protein from the subtilin producing strain Bacillus subtilis ATCC 6633. SpaI is a 16.8-kDa lipoprotein that is attached to the outside of the cytoplasmic membrane via a covalent diacylglycerol anchor. SpaI together with the ABC transporter SpaFEG protects the B. subtilis membrane from subtilin insertion. The solution-NMR structure of a 15-kDa biologically active C-terminal fragment reveals a novel fold. We also demonstrate that the first 20 N-terminal amino acids not present in this C-terminal fragment are unstructured in solution and are required for interactions with lipid membranes. Additionally, growth tests reveal that these 20 N-terminal residues are important for the immunity mediated by SpaI but most likely are not part of a possible subtilin binding site. Our findings are the first step on the way of understanding the immunity mechanism of B. subtilis in particular and of other lantibiotic producing strains in general.

scholarly journals Alanine Esters of Enterococcal Lipoteichoic Acid Play a Role in Biofilm Formation and Resistance to Antimicrobial Peptides

2006 ◽  
Vol 74 (7) ◽  
pp. 4164-4171 ◽  
Author(s):  
Francesca Fabretti ◽  
Christian Theilacker ◽  
Lucilla Baldassarri ◽  
Zbigniew Kaczynski ◽  
Andrea Kropec ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Deletion Mutant ◽  
Lipoteichoic Acid ◽  
Polymyxin B ◽  
Resonance Spectroscopy ◽  
Wild Type ◽  
Gram Positive ◽  
Gram Positive Bacteria ◽  
Surface Molecules ◽  
Environmental Interactions

ABSTRACT Enterococcus faecalis is among the predominant causes of nosocomial infections. Surface molecules like d-alanine lipoteichoic acid (LTA) perform several functions in gram-positive bacteria, such as maintenance of cationic homeostasis and modulation of autolytic activities. The aim of the present study was to evaluate the effect of d-alanine esters of teichoic acids on biofilm production and adhesion, autolysis, antimicrobial peptide sensitivity, and opsonic killing. A deletion mutant of the dltA gene was created in a clinical E. faecalis isolate. The absence of d-alanine in the LTA of the dltA deletion mutant was confirmed by nuclear magnetic resonance spectroscopy. The wild-type strain and the deletion mutant did not show any significant differences in growth curve, morphology, or autolysis. However, the mutant produced significantly less biofilm when grown in the presence of 1% glucose (51.1% compared to that of the wild type); adhesion to eukaryotic cells was diminished. The mutant absorbed 71.1% of the opsonic antibodies, while absorption with the wild type resulted in a 93.2% reduction in killing. Sensitivity to several cationic antimicrobial peptides (polymyxin B, colistin, and nisin) was considerably increased in the mutant strain, confirming similar results from other studies of gram-positive bacteria. Our data suggest that the absence of d-alanine in LTA plays a role in environmental interactions, probably by modulating the net negative charge of the bacterial cell surface, and therefore it may be involved in the pathogenesis of this organism.

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