scholarly journals Full color palette of fluorescentd-amino acids for in situ labeling of bacterial cell walls

2017 ◽  
Vol 8 (9) ◽  
pp. 6313-6321 ◽  
Author(s):  
Yen-Pang Hsu ◽  
Jonathan Rittichier ◽  
Erkin Kuru ◽  
Jacob Yablonowski ◽  
Erick Pasciak ◽  
...  
Keyword(s):  
Amino Acids ◽  
Bacterial Cell ◽  
Cell Walls ◽  
Bacterial Species ◽  
Color Palette ◽  
Full Color ◽  
Bacterial Cell Walls

Fluorescentd-amino acids (FDAAs) enable efficientin situlabeling of peptidoglycan in diverse bacterial species.

scholarly journals Species-Specific Cell Wall Binding Affinity of the S-Layer Proteins of Mosquitocidal Bacterium Bacillus sphaericus C3-41

2009 ◽  
Vol 75 (12) ◽  
pp. 3891-3895 ◽  
Author(s):  
Jia Li ◽  
Xiaomin Hu ◽  
Jianpin Yan ◽  
Zhiming Yuan
Keyword(s):  
Amino Acids ◽  
Cell Wall ◽  
Bacterial Cell ◽  
Cell Walls ◽  
Specific Binding ◽  
Distinct Type ◽  
Bacillus Sphaericus ◽  
Specific Cell ◽  
Bacterial Cell Walls ◽  
Species Specific

ABSTRACT The binding affinities and specificities of six truncated S-layer homology domain (SLH) polypeptides of mosquitocidal Bacillus sphaericus strain C3-41 with the purified cell wall sacculi have been assayed. The results indicated that the SLH polypeptide comprised of amino acids 31 to 210 was responsible for anchoring the S-layer subunits to the rigid cell wall layer via a distinct type of secondary cell wall polymer and that a motif of the recombinant SLH polypeptide comprising amino acids 152 to 210 (rSLH152-210) was essential for the stable binding of the S-layer with the bacterial cell walls. The quantitative assays revealed that the KD (equilibrium dissociation constant) values of rSLH152-210 and rSLH31-210 with purified cell wall sacculi were 1.11 × 10−6 M and 1.40 × 10−6 M, respectively. The qualitative assays demonstrated that the SLH domain of strain C3-41 could bind only to the cell walls or the cells treated with 5 M guanidinium hydrochloride of both toxic and nontoxic B. sphaericus strains but not to those from other bacteria, indicating the species-specific binding of the SLH polypeptide of B. sphaericus with bacterial cell walls.

Factors affecting the susceptibility of bacterial cell walls to the action of lysozyme

1967 ◽  
Vol 167 (1009) ◽  
pp. 446-447 ◽  
Keyword(s):  
Cell Wall ◽  
Bacterial Cell ◽  
Mode Of Action ◽  
Cell Walls ◽  
Bacterial Species ◽  
Bacterial Cell Wall ◽  
Low Molecular Weight ◽  
Factors Affecting ◽  
Structural Differences ◽  
Bacterial Cell Walls

Although we have heard a lot about the mode of binding of low molecular weight, soluble, lysozyme substrates, we have heard little about the mode of action of lysozyme on its natural insoluble substrate, the bacterial cell wall; so I want to bring a biological flavour into this discussion. Lysozyme was the name given by Fleming (1922) to the powerful bacteriolytic agent found in various cells and secretions; it was particularly active against a new bacterial species which he named Micrococcus lysodeikticus . The walls of this species still provide us with one of the best substrates for the study of lysozyme action. Salton showed that there is a considerable spectrum of activity of lysozyme in solubilizing walls of other species of bacteria. For example, walls of M. lysodeikticus are attacked rapidly by a concentration of enzyme of 1 μg/ml., Bacillus megaterium walls need 50 μg/ml., while walls of B. cereus are hardly changed visibly by 50 μg/ml. Consideration of the structure of the basal mucopeptide unit of bacterial cell walls, illustrated by Dr Perkins, shows that there are many ways in which structural differences could be introduced. Knowledge of the effects of some of these differences on lysozyme sensitivity may help in elucidating the mode of action of lysozyme on the complete bacterial cell wall.

scholarly journals Biosynthesis of the Peptidoglycan of Bacterial Cell Walls

1968 ◽  
Vol 243 (11) ◽  
pp. 3169-3179 ◽  
Author(s):  
D J Tipper ◽  
J L Strominger
Keyword(s):  
Bacterial Cell ◽  
Cell Walls ◽  
Bacterial Cell Walls

scholarly journals Structure of N-acetyl-D-alanyl-D-alanine hydrate. An analogue of the COOH-terminal segment of peptidoglycan of bacterial cell walls.

1981 ◽  
Vol 256 (17) ◽  
pp. 9229-9234
Author(s):  
E Benedetti ◽  
B Di Blasio ◽  
V Pavone ◽  
C Pedone ◽  
C Toniolo ◽  
...  
Keyword(s):  
Bacterial Cell ◽  
Cell Walls ◽  
Terminal Segment ◽  
Bacterial Cell Walls

scholarly journals Biosynthesis of the Peptidoglycan of Bacterial Cell Walls

1970 ◽  
Vol 245 (14) ◽  
pp. 3675-3682
Author(s):  
Roland Plapp ◽  
Jack L. Strominger
Keyword(s):  
Bacterial Cell ◽  
Cell Walls ◽  
Bacterial Cell Walls

Biosynthesis of the peptidoglycan of bacterial cell walls

1966 ◽  
Vol 116 ◽  
pp. 487-515 ◽  
Author(s):  
John S. Anderson ◽  
Pauline M. Meadow ◽  
Mary A. Haskin ◽  
Jack L. Strominger
Keyword(s):  
Bacterial Cell ◽  
Cell Walls ◽  
Bacterial Cell Walls

Macrophages produce somnogenic and pyrogenic muramyl peptides during digestion of staphylococci

1991 ◽  
Vol 260 (1) ◽  
pp. R126-R133 ◽  
Author(s):  
L. Johannsen ◽  
J. Wecke ◽  
F. Obal ◽  
J. M. Krueger
Keyword(s):  
Immune Response ◽  
Body Temperature ◽  
Bacterial Cell ◽  
Cell Walls ◽  
Mammalian Cells ◽  
Slow Wave Sleep ◽  
Biological Effects ◽  
Biologically Active ◽  
Chromatographic Behavior ◽  
Bacterial Cell Walls

Muramyl peptides have a variety of biological effects in mammals, including enhancement of the immune response, sleep, and body temperature. Although mammals lack biosynthetic pathways for muramyl peptides, they are found in mammals and are well known as components of bacterial cell walls. This suggests that phagocytic mammalian cells digest bacterial cell walls and produce biologically active muramyl peptides. Staphylococcal cell walls were radioactively labeled during growth of the bacteria. During the digestion of these radiolabeled bacteria, murine bone marrow macrophages produced low-molecular-weight substances that coeluted chromatographically with the radioactive cell wall marker. Further separation of these substances using reversed-phase high-performance liquid chromatography resulted in the isolation of substances with high specific biological activity. Intracerebroventricular injection of rabbits with these substances induced an increase in slow-wave sleep and body temperature and a suppression of rapid-eye-movement sleep. The characteristics of the biological responses and the chromatographic behavior of the active components are consistent with those of muramyl peptides. The ability of macrophages to tailor muramyl peptides from peptidoglycan may provide an amplification step for the immune response. Muramyl peptides released by macrophages may also act as mediators for various facets of the acute phase response elicited by bacterial infections such as fever and sleep.

EXTRACELLULAR ENZYMES FROM STRAINS OF SORANGIUM

1965 ◽  
Vol 11 (1) ◽  
pp. 109-118 ◽  
Author(s):  
D. C. Gillespie ◽  
F. D. Cook
Keyword(s):  
Bacterial Cell ◽  
Cell Walls ◽  
Extracellular Enzymes ◽  
Soil Organisms ◽  
Wide Range ◽  
Bacterial Cell Walls

Soil organisms belonging to the myxobacter group and predatory on molds, yeasts, nematodes, and streptomycetes as well as on a wide range of bacteria elaborate at least two extracellular enzymes: a protease and a lysin. The protease hydrolyzes casein and haemoglobin and is inactive against bacterial cell walls while the lysin hydrolyzes bacterial cell walls but is inactive on proteins. These enzymes have been separated on hydroxylapatite columns and some of their properties are described. The predatory action of many of the isolates may be explained by the secretion and subsequent action of these two enzymes.

Sign in / Sign up

Export Citation Format

Share Document