scholarly journals The N-terminal peptide moiety of theMycobacterium tuberculosis19 kDa lipoprotein harbors RP105-agonistic properties

2018 ◽  
Vol 103 (2) ◽  
pp. 311-319
Author(s):  
Thomas E. Schultz ◽  
Karl-Heinz Wiesmüller ◽  
Megan Lucas ◽  
Karen M. Dobos ◽  
Alan G. Baxter ◽  
...  
Keyword(s):  
Peptide Moiety

scholarly journals Synthetic lipopeptide Pam3CysSer(Lys)4 is an effective activator of human platelets

1994 ◽  
Vol 266 (6) ◽  
pp. C1684-C1691 ◽  
Author(s):  
M. Berg ◽  
S. Offermanns ◽  
R. Seifert ◽  
G. Schultz
Keyword(s):  
Calcium Concentration ◽  
Cytosolic Calcium ◽  
Human Platelets ◽  
Cellular Effects ◽  
Prostacyclin Receptor ◽  
Serotonin Secretion ◽  
Peptide Moiety ◽  
Lipid Moiety ◽  
Molecular Masses ◽  
Aggregation Of Platelets

Lipopeptide analogues of the NH2-terminus of bacterial lipoprotein are known to induce activation of macrophages, neutrophils, and lymphocytes. We studied the effect of the lipopeptide N-palmitoyl-S-[2,3-bis(palmitoyloxy)-(2RS)-propyl]-(R)-cysteinyl-( S)-seryl-(S)-lysyl-(S)-lysyl-(S)-lysyl-(S)-lysine [Pam3CysSer(Lys)4] on several functions of human platelets. Pam3CysSer(Lys)4 led to the aggregation of platelets and induced the secretion of serotonin with an effectiveness similar to thrombin. These cellular effects of Pam3CysSer(Lys)4 were concentration dependent, being half maximal at 2-3 microM and maximal at 10-30 microM. Another lipopeptide also induced platelet aggregation and serotonin secretion but was less potent and less effective than Pam3CysSer(Lys)4. The lipid moiety and the peptide moiety of Pam3CysSer(Lys)4 alone were without any effect. Lipopeptides also stimulated tyrosine phosphorylation of several proteins with molecular masses similar to those found to be tyrosine phosphorylated in response to thrombin, and Pam3CysSer(Lys)4 led to an increase in the cytosolic calcium concentration. All studied responses of platelets to lipopeptides were inhibited by the prostacyclin receptor agonist cicaprost. Taken together, our data show that lipopeptides are effective activators of human platelets and that this activation is susceptible to the action of physiological platelet inhibitors.

Release of soluble peptidoglycan from growing conococci: demonstration of anhydro-muramyl-containing fragments

1980 ◽  
Vol 29 (3) ◽  
pp. 914-925 ◽  
Author(s):  
R K Sinha ◽  
R S Rosenthal
Keyword(s):  
Group Analysis ◽  
Gel Filtration ◽  
Diaminopimelic Acid ◽  
Host Interactions ◽  
Peptide Moiety ◽  
Kd Values ◽  
Monomer Fraction ◽  
Combined Action ◽  
Beta Elimination

Previous analysis of soluble peptidoglycan (PG) fragments released by exponentially growing gonococci implicated the combined action of both hexosaminidase and amidase activities in PG turnover. Current studies further characterized PG fragments which were labeled in the glycan with D-glucosamine and in the peptide moiety with meso-diaminopimelic acid of L- and D-alanine. Labeled PG fragments were isolated by gel filtration and characterized on the bases of (i) KD values, (ii) free amino group analysis using fluorodinitrobenzene, (iii) borohydride reduction, (iv) alkali-catalyzed beta-elimination, (v) paper chromatography in various solvents, (vi) electrophoretic mobility at various pH values, (vii) digestibility by Charonia lampas glycosidases, and (viii) content of labeled D- and L-alanine. A set of well-characterized PG fragments was used as standards. The monomer fraction (the major extracellular product) was found to contain two components. Most (about 80%) appeared to be N-acetylglucosaminyl-beta-1 leads to 4-1,6-anhydro-N-acetylmuramyl-L-ala-D-glu-meso-diaminopimelic acid; the remainder was the corresponding disaccharide tetrapeptide containing a C-terminal D-alanine. An unusual feature of these products was the presence of the anhydro-muramyl (non-reducing) ends, reflecting the activity of a gonococcal transglycosylase, and the near absence of products containing detectable reducing ends. Otherwise, the structures of the monomer fragments were typical of those expected for a gram-negative bacterium (chemotype I). The corresponding peptide-cross-linked dimer and the free disaccharide also contained nonreducing ends, exclusively. Free peptides (products of amidase activity) consisted of both tripeptide and tetrapeptide. In summary, all gonococci examined appear to possess an unusual transglycosylase activity which contributes to the release of soluble PG fragments containing nonreducing, anhydro-muramyl ends. The release of these fragments in vivo might be a unique aspect of gonococci-host interactions.

scholarly journals Amino Acid Residues Required for Maturation, Cell Uptake, and Processing of Translation Inhibitor Microcin C

2006 ◽  
Vol 189 (5) ◽  
pp. 2114-2118 ◽  
Author(s):  
Teymur Kazakov ◽  
Anastasia Metlitskaya ◽  
Konstantin Severinov
Keyword(s):  
Amino Acid ◽  
Trna Synthetase ◽  
Trojan Horse ◽  
Cell Uptake ◽  
Amino Acid Residues ◽  
Peptide Moiety ◽  
Translation Inhibitor ◽  
Mutational Study ◽  
The Way

ABSTRACT Microcin C (McC), a peptide-nucleotide Trojan horse antibiotic, targets aspartyl-tRNA synthetase. We present the results of a systematic mutational study of the 7-amino-acid ribosomally synthesized peptide moiety of McC. Our results define amino acid positions important for McC maturation and cell uptake and processing and open the way for creation of more potent McC-based inhibitors.

scholarly journals Antibiotic and Biosurfactant Properties of Cyclic Lipopeptides Produced by Fluorescent Pseudomonas spp. from the Sugar Beet Rhizosphere

2002 ◽  
Vol 68 (7) ◽  
pp. 3416-3423 ◽  
Author(s):  
T. H. Nielsen ◽  
D. Sørensen ◽  
C. Tobiasen ◽  
J. B. Andersen ◽  
C. Christophersen ◽  
...  
Keyword(s):  
Amino Acids ◽  
Biological Control ◽  
Cyclic Peptide ◽  
Agricultural Soils ◽  
Pathogenic Fungi ◽  
Growth Media ◽  
Single Strain ◽  
Cyclic Lipopeptides ◽  
Peptide Moiety

ABSTRACT Cyclic lipopeptides (CLPs) with antibiotic and biosurfactant properties are produced by a number of soil bacteria, including fluorescent Pseudomonas spp. To provide new and efficient strains for the biological control of root-pathogenic fungi in agricultural crops, we isolated approximately 600 fluorescent Pseudomonas spp. from two different agricultural soils by using three different growth media. CLP production was observed in a large proportion of the strains (approximately 60%) inhabiting the sandy soil, compared to a low proportion (approximately 6%) in the loamy soil. Chemical structure analysis revealed that all CLPs could be clustered into two major groups, each consisting of four subgroups. The two major groups varied primarily in the number of amino acids in the cyclic peptide moiety, while each of the subgroups could be differentiated by substitutions of specific amino acids in the peptide moiety. Production of specific CLPs could be affiliated with Pseudomonas fluorescens strain groups belonging to biotype I, V, or VI. In vitro analysis using both purified CLPs and whole-cell P. fluorescens preparations demonstrated that all CLPs exhibited strong biosurfactant properties and that some also had antibiotic properties towards root-pathogenic microfungi. The CLP-producing P. fluorescens strains provide a useful resource for selection of biological control agents, whether a single strain or a consortium of strains was used to maximize the synergistic effect of multiple antagonistic traits in the inoculum.

Effect of the Peptide Moiety of Lipid II on Bacterial Transglycosylase

2012 ◽  
Vol 124 (40) ◽  
pp. 10270-10273 ◽  
Author(s):  
Hao-Wei Shih ◽  
Yi-Fan Chang ◽  
Wei-Jing Li ◽  
Fan-Chun Meng ◽  
Chia-Ying Huang ◽  
...  
Keyword(s):  
Lipid Ii ◽  
Peptide Moiety

scholarly journals Detection, purification and characterization of a human cancer-associated galactosyltransferase acceptor

1979 ◽  
Vol 178 (2) ◽  
pp. 279-287 ◽  
Author(s):  
D K Podolsky ◽  
M M Weiser
Keyword(s):  
Molecular Weight ◽  
Human Cancer ◽  
Deae Cellulose ◽  
Structural Data ◽  
Low Molecular Weight ◽  
Gel Chromatography ◽  
Purification And Characterization ◽  
Peptide Moiety ◽  
Cellulose Column

A low-molecular-weight acceptor of galactosyltransferase activity was detected in sera and effusions of patients with extensive maligant disease. This substance was purified to homogeneity from both human serum and effusion by using sequential charcoal/Celite and DEAE-cellulose column chromatography. The purified acceptor was shown to act as substrate for both purified normal and cancer-associated human galactosyltransferase (EC 2.4.1.22) isoenzymes, but had a higher affinity for the cancer-associated isoenzyme (Km = 20 microM) than for the normal isoenzyme (Km = 500 microM). The substrate was found to be a glycopeptide with mol.wt. approx. 3600 determined by polyacrylamide-gel chromatography. Carbohyydate analysis demonstrated only the presence of glucosamine and mannose. Amino acid analysis revealed that the peptide moiety consisted of eight different amino acids, including two residues of asparagine and one residue of serine, but no threonine. These structural data suggest that the acceptor is a fraction of an asparagine-glucosamine type of glycoprotein.

Chemical characterization of urinary glycopeptides.

1987 ◽  
Vol 33 (12) ◽  
pp. 2214-2219
Author(s):  
H Matsue ◽  
K Takagaki ◽  
K Honda ◽  
Y Nakagawa ◽  
F Gejyo ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Carbohydrate Chain ◽  
Cetylpyridinium Chloride ◽  
Gel Filtration ◽  
Chemical Characterization ◽  
Small Peptide ◽  
Supernatant Liquid ◽  
Peptide Moiety ◽  
Peptide Linkage

Abstract We prepared human urinary glycopeptides from the supernatant liquid remaining after precipitation of the nondialyzable fraction with cetylpyridinium chloride. Using cation exchange and affinity chromatographies and gel filtration, we obtained 28 glycopeptide subfractions. By compositional analyses of sugar and amino acid, and by reducing-terminal analyses after reduction with NaBH4, we determined the size of the carbohydrate moiety and the types of carbohydrate-peptide linkage involved. We isolated several glycopeptides not previously described: six with sialic acid, two with fucose, two with glucose, and one with N-acetylgalactosamine. The sialic acid glycopeptides had a short carbohydrate chain of the O-glycoside type. The fucose-containing glycopeptides were fucosyllactosaminoglycans. The glucose glycopeptides were polymers linked to a small peptide moiety. The N-acetylgalactosamine-rich glycopeptide was found in an N-glycoside-type fraction, with N-acetylgalactosamine at the nonreducing terminal.

Die Aminosäuresequenz des Asparaginsäure enthaltenden Mureins von Lactobacillus coryniformis und Lactobacillus cellobiosus

1967 ◽  
Vol 22 (10) ◽  
pp. 1062-1067 ◽  
Author(s):  
Roland Plapp ◽  
Otto Kandler
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Aspartic Acid ◽  
Cell Walls ◽  
Peptide Bond ◽  
Partial Hydrolysis ◽  
Cross Linking ◽  
Peptide Moiety ◽  
Lactobacillus Coryniformis ◽  
Hydrolysis Of

The amino acid sequence of the peptide moiety of the mureins of Lactobacillus coryniformis and Lactobacillus cellobiosus cell walls was determined. This was accomplished by the identification of peptides obtained after partial hydrolysis of purified cell walls and by the identification of UDP-activated murein precursors accumulated by ᴅ-cycloserine inhibition. The amino acid sequence proved to be : ʟ-ala-ᴅ-glu-ʟ-lys-ᴅ-ala for L. coryniformis and L-ala-D-glu-L-orn-D-ala for L. cellobio-.D-asp D-aspsus. Aspartic acid is involved in the cross-linking of the mureins by forming a peptide bond with the C-terminal D-alanine of an adjacent muropeptide. Glutamic acid as well as aspartic acid are present as amides.

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