Chemical Structure of Bacterial Cell Walls: Amino-acids of Walls of Micrococcus radiodurans

Nature ◽  
1964 ◽  
Vol 201 (4924) ◽  
pp. 1107-1109 ◽  
Author(s):  
ELIZABETH WORK
2017 ◽  
Vol 8 (9) ◽  
pp. 6313-6321 ◽  
Author(s):  
Yen-Pang Hsu ◽  
Jonathan Rittichier ◽  
Erkin Kuru ◽  
Jacob Yablonowski ◽  
Erick Pasciak ◽  
...  

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


2000 ◽  
Vol 68 (6) ◽  
pp. 3535-3540 ◽  
Author(s):  
Egle Šimelyte ◽  
Marja Rimpiläinen ◽  
Leena Lehtonen ◽  
Xiang Zhang ◽  
Paavo Toivanen

ABSTRACT To study what determines the arthritogenicity of bacterial cell walls, cell wall-induced arthritis in the rat was applied, using four strains of Lactobacillus. Three of the strains used proved to induce chronic arthritis in the rat; all were Lactobacillus casei. The cell wall of Lactobacillus fermentum did not induce chronic arthritis. All arthritogenic bacterial cell walls had the same peptidoglycan structure, whereas that of L. fermentum was different. Likewise, all arthritogenic cell walls were resistant to lysozyme degradation, whereas the L. fermentum cell wall was lysozyme sensitive. Muramic acid was observed in the liver, spleen, and lymph nodes in considerably larger amounts after injection of an arthritogenicL. casei cell wall than following injection of a nonarthritogenic L. fermentum cell wall. The L. casei cell wall also persisted in the tissues longer than theL. fermentum cell wall. The present results, taken together with those published previously, underline the possibility that the chemical structure of peptidoglycan is important in determining the arthritogenicity of the bacterial cell wall.


2009 ◽  
Vol 75 (12) ◽  
pp. 3891-3895 ◽  
Author(s):  
Jia Li ◽  
Xiaomin Hu ◽  
Jianpin Yan ◽  
Zhiming Yuan

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.


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

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

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

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