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Autor:Hansenová Manásková S; Nazmi K; van 't Hof W; van Belkum A; Martin NI; Bikker FJ; van Wamel WJ; Veerman ECEndere?o:Department of Periodontology and Oral Biochemistry, Academic Centre for Dentistry Amsterdam (ACTA), University of Amsterdam and VU University Amsterdam, Amsterdam, The Netherlands.
Título:Staphylococcus aureus Sortase A-Mediated Incorporation of Peptides: Effect of Peptide Modification on Incorporation.
Fonte:PLoS O 11(1):e16.
ISSN:País de publica??o:United States
Idioma:ENGResumo:The endogenous Staphylococcus aureus sortase A (SrtA) transpeptidase covalently anchors cell wall-anchored (CWA) proteins equipped with a specific recognition motif (LPXTG) into the peptidoglycan layer of the staphylococcal cell wall. Previous in situ experiments have shown that SrtA is also able to incorporate exogenous, fluorescently labelled, synthetic substrates equipped with the LPXTG motif (K(FITC)LPETG-amide) into the bacterial cell wall, albeit at high concentrations of 500 uM to 1 mM. In the present study, we have evaluated the effect of substrate modification on the incorporation efficiency. This revealed that (i) by elongation of LPETG-amide with a sequence of positively charged amino acids, derived from the C-terminal domain of physiological SrtA substrates, the incorporation efficiency was increased by 20-fold at 10 uM, 100 uM and 250 uM; (ii) Substituting aspartic acid (E) for methionine increased the incorporation of the resulting K(FITC)LPMTG-amide approximately three times at all c (iii) conjugation of the lipid II binding antibiotic vancomycin to K(FITC)LPMTG-amide resulted in the same incorporation levels as K(FITC)LPETG-amide, but much more efficient at an impressive 500-fold lower substrate concentration. These newly developed synthetic substrates can potentially find broad applications in for example the in situ the incorporation of antibody the targeted delivery and covalent incorporation of antimicrobial compounds into the bacterial cell wall.
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de subst?ncia:0 (Anti-Bacterial Agents); 0 (Bacterial Proteins); 0 (Peptides); 0 (RNA Recognition Motif Proteins); 6Q205EH1VU (Vancomycin); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases)
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Autor:Hay ID; Du J; Reyes PR; Rehm BHEndere?o:Department of Microbiology, Monash University, Clayton, 3800, Australia. iain.hay@monash.edu.
Título:In vivo polyester immobilized sortase for tagless protein purification.
Fonte:Microb Cell F 14:190, 2015 Nov 25.
ISSN:País de publica??o:England
Idioma:ENGResumo:BACKGROUND: Laboratory scale recombinant protein production and purification techniques are often complicated, involving multiple chromatography steps and specialized equipment and reagents. Here it was demonstrated that recombinant proteins can be expressed as covalently immobilized to the surface of polyester (polyhydroxyalkanoate, PHA) beads in vivo in Escherichia coli by genetically fusing them to a polyester synthase gene (phaC). The insertion of a self-cleaving module, a modified sortase A (SrtA) from Staphylococcus aureus and its five amino acid recognition sequence between the synthase and the target protein led to a simple protein production and purification method. RESULTS: The generation of hybrid genes encoding tripartite PhaC-SrtA-Target fusion proteins, enabled immobilization of proteins of interest to the surface of PHA beads in vivo. After simple cell lysis and isolation of the PHA beads, the target proteins could be selectively and efficiently released form the beads by activating the sortase with CaCl2 and triglycine. Up to 6 mg/l of soluble proteins at a purity of ~98 % could be isolated in one step with no optimization. This process was used to produce and isolate three proteins: Green fluorescent protein, maltose binding protein and the Mycobacterium tuberculosis vaccine candidate Rv1626. CONCLUSIONS: We have developed a new technique for easy production and purification of recombinant proteins. This technique is capable of producing and purifying high yields of proteins suitable for research application in less than 2 days. No costly or specialized protein chromatography equipment, resins, reagents or expertise are required.
Tipo de publica??o: JOURNAL ARTICLE
Nome de subst?ncia:0 (Bacterial Proteins); 0 (Maltose-Binding Proteins); 0 (Oligopeptides); 0 (Polyesters); 0 (Recombinant Fusion Proteins); -9 (Green Fluorescent Proteins); CVK73ZDQ8B (glycyl-glycyl-glycine); EC 2.3.- (Acyltransferases); EC 2.3.1.- (poly(3-hydroxyalkanoic acid) synthase); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases); M4I0D6VV5M (Calcium Chloride)
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Autor:Beerli RR; Hell T; Merkel AS; Grawunder UEndere?o:NBE-Therapeutics AG, Hochbergerstrasse, Basel, Switzerland.
Título:Sortase Enzyme-Mediated Generation of Site-Specifically Conjugated Antibody Drug Conjugates with High In Vitro and In Vivo Potency.
Fonte:PLoS O 10(7):e15.
ISSN:País de publica??o:United States
Idioma:ENGResumo:Antibody drug conjugates (ADCs) have recently been proven to be highly potent anti-tumor drugs, typically exceeding the efficacy of conventional monoclonal antibodies (mAbs). ADCs are currently produced by chemical conjugation of a small-molecule toxin to the mAb through lysine or cysteine side chains. This leads to heterogeneous mixtures of ADCs in which variable numbers of drugs are conjugated to individual antibodies and in which the site of conjugation cannot be defined. Consequently, there is currently significant interest in further development of drug conjugation technologies, with a particular focus on site-specific payload conjugation. Here, we present an enzymatic conjugation platform based on the S. aureus sortase A-mediated transpeptidation reaction, allowing the efficient generation of ADCs with toxins conjugated to pre-defined sites at pre-defined drug-to-antibody ratios. For this, two modifications were introduced: first, immunoglobulin heavy (IgH) and light (IgL) chains were modified at their C-termini by addition of the sortase A recognition motif LPETG, and second, the small molecule tubulin polymerization inhibitors monomethylauristatin E (MMAE) and maytansine were modified by addition of a pentaglycine peptide, thus making them suitable substrates for sortase A-mediated transpeptidation. We demonstrate efficient generation and characterization of the anti-CD30 ADC Ac10-vcPAB-MMAE, an enzymatically conjugated counterpart of brentuximab vedotin (Adcetris), as well as several anti-HER-2 ADCs including trastuzumab-maytansine, the counterpart of trastuzumab emtansine (Kadcyla). ADCs generated in this manner were found to display in vitro cell killing activities indistinguishable from the classic conjugates. Further, when tested in vivo in a HER-2-overexpressing ovarian cancer xenograft mouse model, enzymatically generated trastuzumab-maytansine was found to lead to complete regression of established tumors, similar to Kadcyla.
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de subst?ncia:0 (Antibodies, Monoclonal); 0 (Antibodies, Monoclonal, Humanized); 0 (Antigens, CD30); 0 (Antineoplastic Agents); 0 (Bacterial Proteins); 0 (Immunoconjugates); 0 (Oligopeptides); 0 (monomethyl auristatin E); 1 (Maytansine); 7XL5ISS668 (brentuximab vedotin); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 2.7.10.1 (ERBB2 protein, human); EC 2.7.10.1 (Receptor, ErbB-2); EC 3.4.22.- (Cysteine Endopeptidases); SE2KH7T06F (ado-trastuzumab emtansine)
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Autor:Yu LX; Tao Y; Qiu RM; Zhou Y; Zhi QH; Lin HCEndere?o:Department of Preventive Dentistry, Guanghua School of Stomatology, Sun Yat-Sen University, 56 Ling Yuan Road West, Guangzhou, China. Yuu_.
Título:Genetic polymorphisms of the sortase A gene and social-behavioural factors associated with caries in children: a case-control study.
Fonte:BMC Oral H 15:54, 2015 May 02.
ISSN:País de publica??o:England
Idioma:ENGResumo:BACKGROUND: Streptococcus mutans (S. mutans) is the primary etiological agent of dental caries. Sortase is a transpeptidase that anchors several surface proteins to the S. mutans cell wall and has been shown to play a major role in cariogenicity. The purpose of this study was to explore the genetic polymorphisms of the sortase gene (srtA) and the social-behavioural factors associated with dental caries in children with S. mutans. METHODS: In this case-control study, 121 S. mutans strains were separately selected from caries-free children and high-severity caries children for sequencing of the srtA gene. Social and behavioural data were collected by self-administered questionnaires. Genomic DNA was extracted from S. mutans strains and amplified by PCR to obtain the srtA gene. The purified PCR products were sequenced and analysed for mutations with ABI Variant Reporter software. The distribution of missense mutations and the mean of social-behavioural factors were compared between the groups. A multiple logistic regression model was used to control for confounding factors. RESULTS: The mutation frequencies at loci 168 (P = 0.023) and 470 (P = 0.032) were significantly different between the groups. The best-fitting model showed that greater age, high frequencies of solid sugar consumption, prolonged breastfeeding, a high proportion of visible plaque, and S. mutans with a T at locus 168 of the srtA gene were associated with high-severity caries in children (P < 0.05). Children carrying a G at locus 168 of S. mutans had a decreased risk for high-severity caries (OR = 0.32, 95% CI = 0.12-0.86) compared with those carrying a T. CONCLUSIONS: The present study suggested that the locus 168 missense mutation of the srtA gene may correlate with caries susceptibility in children with S. mutans. In addition, age, duration of breastfeeding, solid sugar consumption, and poor oral hygiene contributed to this complex disease.
Tipo de publica??o: COMPARATIVE STUDY; JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de subst?ncia:0 (Bacterial Proteins); 0 (Dietary Sucrose); 0 (Peptidoglycan); 5Z93L87A1R (Guanine); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases); QR26YLT7LT (Thymine)
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Autor:Zhang H; Deery MJ; Gannon L; Powers SJ; Lilley KS; Theodoulou FLEndere?o:Biological Chemistry and Crop Protection Department, Rothamsted Research, Harpenden, UK.
Título:Quantitative proteomics analysis of the Arg/N-end rule pathway of targeted degradation in Arabidopsis roots.
Fonte:P 15(14):15 Jul.
ISSN:País de publica??o:Germany
Idioma:ENGResumo:According to the Arg/N-end rule pathway, proteins with basic N-termini are targeted for degradation by the Arabidopsis thaliana E3 ligase, PROTEOLYSIS6 (PRT6). Proteins can also become PRT6 substrates following post-translational arginylation by arginyltransferases ATE1 and 2. Here, we undertook a quantitative proteomics study of Arg/N-end rule mutants, ate1/2 and prt6, to investigate the impact of this pathway on the root proteome. Tandem mass tag labelling identified a small number of proteins with increased abundance in the mutants, some of which represent downstream targets of transcription factors known to be N-end rule substrates. Isolation of N-terminal peptides using terminal amine isotope labelling of samples (TAILS) combined with triple dimethyl labelling identified 1465 unique N-termini. Stabilising residues were over-represented among the free neo-N-termini, but destabilising residues were not markedly enriched in N-end rule mutants. The majority of free neo-N-termini were revealed following cleavage of organellar targeting signals, thus compartmentation may account in part for the presence of destabilising residues in the wild-type N-terminome. Our data suggest that PRT6 does not have a marked impact on the global proteome of Arabidopsis roots and is likely involved in the controlled degradation of relatively few regulatory proteins. All MS data have been deposited in the ProteomeXchange with identifier PXD001719 (http://proteomecentral.proteomexchange.org/dataset/PXD001719).
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de subst?ncia:0 (Arabidopsis Proteins); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.27 (PRT6 protein, Arabidopsis); EC 2.3.2.27 (Ubiquitin-Protein Ligases); EC 2.3.2.8 (arginyltransferase)
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Autor:Del Tordello E; Danilchanka O; McCluskey AJ; Mekalanos JJEndere?o:Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115.
Título:Type VI secretion system sheaths as nanoparticles for antigen display.
Fonte:Proc Natl Acad Sci U S A; 113(11):16 Mar 15.
ISSN:País de publica??o:United States
Idioma:ENGResumo:The bacterial type 6 secretion system (T6SS) is a dynamic apparatus that translocates proteins between cells by a mechanism analogous to phage tail contraction. T6SS sheaths are cytoplasmic tubular structures composed of stable VipA-VipB (named for ClpV-interacting protein A and B) heterodimers. Here, the structure of the VipA/B sheath was exploited to generate immunogenic multivalent particles for vaccine delivery. Sheaths composed of VipB and VipA fused to an antigen of interest were purified from Vibrio cholerae or Escherichia coli and used for immunization. Sheaths displaying heterologous antigens generated better immune responses against the antigen and different IgG subclasses compared with soluble antigen alone. Moreover, antigen-specific antibodies raised against sheaths presenting Neisseria meningitidis factor H binding protein (fHbp) antigen were functional in a serum bactericidal assay. Our results demonstrate that multivalent nanoparticles based on the T6SS sheath represent a versatile scaffold for vaccine applications.
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de subst?ncia:0 (Antibodies, Bacterial); 0 (Antigens); 0 (Antigens, Bacterial); 0 (Bacterial Proteins); 0 (Bacterial Vaccines); 0 (Immunoglobulin G); 0 (Recombinant Fusion Proteins); 0 (Type VI Secretion Systems); 0 (Vaccines); 0 (factor H-binding protein, Neisseria meningitidis); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases)
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Autor:Liu YJ; Liu C; Chang Z; Wadas B; Brower CS; Song ZH; Xu ZL; Shang YL; Liu WX; Wang LN; Dong W; Varshavsky A; Hu RG; Li WEndere?o:From the State Key Laboratory of Stem Cell and Reproductive Biology, Institute of Zoology, Chinese Academy of Sciences, Beijing 100101, China, the College of Marine Life, Ocean University of China, Qingdao 266003, China, and.
Título:Degradation of the Separase-cleaved Rec8, a Meiotic Cohesin Subunit, by the N-end Rule Pathway.
Fonte:J Biol C 291(14):16 Apr 1.
ISSN:XPaís de publica??o:United States
Idioma:ENGResumo:The Ate1 arginyltransferase (R-transferase) is a component of the N-end rule pathway, which recognizes proteins containing N-terminal degradation signals called N-degrons, polyubiquitylates these proteins, and thereby causes their degradation by the proteasome. Ate1 arginylates N-terminal Asp, Glu, or (oxidized) Cys. The resulting N-terminal Arg is recognized by ubiquitin ligases of the N-end rule pathway. In the yeastSaccharomyces cerevisiae, the separase-mediated cleavage of the Scc1/Rad21/Mcd1 cohesin subunit generates a C-terminal fragment that bears N-terminal Arg and is destroyed by the N-end rule pathway without a requirement for arginylation. In contrast, the separase-mediated cleavage of Rec8, the mammalian meiotic cohesin subunit, yields a fragment bearing N-terminal Glu, a substrate of the Ate1 R-transferase. Here we constructed and used a germ cell-confinedAte1(-/-)mouse strain to analyze the separase-generated C-terminal fragment of Rec8. We show that this fragment is a short-lived N-end rule substrate, that its degradation requires N-terminal arginylation, and that maleAte1(-/-)mice are nearly infertile, due to massive apoptotic death ofAte1(-/-)spermatocytes during the metaphase of meiosis I. These effects ofAte1ablation are inferred to be caused, at least in part, by the failure to destroy the C-terminal fragment of Rec8 in the absence of N-terminal arginylation.
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
Nome de subst?ncia:0 (Nuclear Proteins); 0 (Phosphoproteins); 0 (Rad21 protein, mouse); 0 (Rec8 protein, mouse); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.8 (arginyltransferase); EC 3.4.22.49 (Separase)
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Autor:Chan AH; Yi SW; Terwilliger AL; Maresso AW; Jung ME; Clubb RTEndere?o:From the Department of Chemistry and Biochemistry, UCLA-DOE Institute of Genomics and Proteomics, and the Molecular Biology Institute, University of California, Los Angeles, California 90095 and.
Título:Structure of the Bacillus anthracis Sortase A Enzyme Bound to Its Sorting Signal: A FLEXIBLE AMINO-TERMINAL APPENDAGE MODULATES SUBSTRATE ACCESS.
Fonte:J Biol C 290(42):15 Oct 16.
ISSN:País de publica??o:United States
Idioma:ENGResumo:The endospore forming bacterium Bacillus anthracis causes lethal anthrax disease in humans and animals. The ability of this pathogen to replicate within macrophages is dependent upon the display of bacterial surface proteins attached to the cell wall by the B. anthracis Sortase A ((Ba)SrtA) enzyme. Previously, we discovered that the class A (Ba)SrtA sortase contains a unique N-terminal appendage that wraps around the body of the protein to contact the active site of the enzyme. To gain insight into its function, we determined the NMR structure of (Ba)SrtA bound to a LPXTG sorting signal analog. The structure, combined with dynamics, kinetics, and whole cell protein display data suggest that the N terminus modulates substrate access to the enzyme. We propose that it may increase the efficiency of protein display by reducing the unproductive hydrolytic cleavage of enzyme-protein covalent intermediates that form during the cell wall anchoring reaction. Notably, a key active site loop (ss7/ss8 loop) undergoes a disordered to ordered transition upon binding the sorting signal, potentially facilitating recognition of lipid II.
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
Nome de subst?ncia:0 (Bacterial Proteins); 0 (Protein Sorting Signals); EC 2.3.2.- (Aminoacyltransferases); EC 2.3.2.- (sortase A); EC 3.4.22.- (Cysteine Endopeptidases)
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Autor:Peltier J; Shaw HA; Couchman EC; Dawson LF; Yu L; Choudhary JS; Kaever V; Wren BW; Fairweather NFEndere?o:From the Department of Life Sciences, Center for Molecular Bacteriology and Infection, Imperial College London, London SW7 2AZ, United Kingdom.
Título:Cyclic diGMP regulates production of sortase substrates of Clostridium difficile and their surface exposure through ZmpI protease-mediated cleavage.
Fonte:J Biol C 290(40):15 Oct 2.
ISSN:XPaís de publica??o:United States
Idioma:ENGResumo:In Gram-positive pathogens, surface proteins may be covalently anchored to the bacterial peptidoglycan by sortase, a cysteine transpeptidase enzyme. In contrast to other Gram-positive bacteria, only one single sortase enzyme, SrtB, is conserved between strains of Clostridium difficile. Sortase-mediated peptidase activity has been reported in vitro, and seven potential substrates have been identified. Here, we demonstrate the functionality of sortase in C. difficile. We identify two sortase-anchored proteins, the putative adhesins CD2831 and CD3246, and determine the cell wall anchor structure of CD2831. The C-terminal PPKTG sorting motif of CD2831 is cleaved between the threonine and glycine residues, and the carboxyl group of threonine is amide-linked to the side chain amino group of diaminopimelic acid within the peptidoglycan peptide stem. We show that CD2831 protein levels are elevated in the presence of high intracellular cyclic diGMP (c-diGMP) concentrations, in agreement with the control of CD2831 expression by a c-diGMP-dependent type II riboswitch. Low c-diGMP levels induce the release of CD2831 and presumably CD3246 from the surface of cells. This regulation is mediated by proteolytic cleavage of CD2831 and CD3246 by the zinc metalloprotease ZmpI, whose expression is controlled by a type I c-diGMP riboswitch. These data reveal a novel regulatory mechanism for expression of two sortase substrates by the secondary messenger c-diGMP, on which surface anchoring is dependent.
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de subst?ncia:0 (Adhesins, Bacterial); 0 (Bacterial Proteins); 0 (Oligonucleotides); 0 (Peptidoglycan); 0 (Virulence Factors);
(bis(3',5')-cyclic diguanylic acid); EC 2.3.2.- (Aminoacyltransferases); EC 3.4.- (Metalloproteases); EC 3.4.- (Peptide Hydrolases); EC 3.4.22.- (Cysteine Endopeptidases); H2D2X058MU (Cyclic GMP)
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Autor:Chambers CJ; Roberts AK; Shone CC; Acharya KREndere?o:1] Public Health England, Porton Down, Salisbury SP4 0JG, UK [2] Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK.
Título:Structure and function of a Clostridium difficile sortase enzyme.
Fonte:Sci R 5: Mar 24.
ISSN:País de publica??o:England
Idioma:ENGResumo:Sortase enzymes are responsible for covalent anchoring of specific proteins to the peptidoglycan of the cell wall of gram-positive bacteria. In some gram-positive bacteria (e.g. Staphylococcus aureus), sortases have been found to be essential for pathogenesis and their inhibitors are under development as potential novel therapeutics. Here we provide the first report on the structural characterisation of the C. difficile sortase. An active site mutant was crystallised and its structure determined to 2.55 ? by X-ray diffraction to provide structural insight into its catalytic mechanism. In order to elucidate the role of the sortase in the cell wall biogenesis, a C. difficile sortase knockout strain was constructed by intron mutagenesis. Characterisation of this mutant led to the discovery that the putative adhesin CD0386 is anchored to the peptidoglycan of C. difficile by the sortase SrtB and that an SPKTG peptide motif is involved in the transpeptidation reaction with the C. difficile peptidoglycan. In an animal model for C. difficile infection, the SrtB mutant caused disease at a similar rate of onset as the wild type strain. In conclusion, our detailed study shows that the SrtB enzyme from C. difficile does not play an essential role in pathogenesis.
Tipo de publica??o: JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Nome de subst?ncia:0 (Bacterial Proteins); 0 (sortase B); EC 2.3.2.- (Aminoacyltransferases); EC 3.4.22.- (Cysteine Endopeptidases)
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