scholarly journals Extraction, purification and characterization of a peptidoglycan hydrolase from vegetative cells of Clostridium perfringens type A.

1990 ◽  
Vol 36 (5) ◽  
pp. 333-344
Author(s):  
RONALD G. LABBÉ ◽  
HSIAO-PING LU ◽  
SHIRLEY TANG
Keyword(s):  
Clostridium Perfringens ◽  
Type A ◽  
Peptidoglycan Hydrolase ◽  
Purification And Characterization ◽  
Vegetative Cells

Purification and characterization of a recombinant α-N-acetylgalactosaminidase from Clostridium perfringens

2003 ◽  
Vol 32 (2) ◽  
pp. 309-316 ◽  
Author(s):  
Hsin-Yeh Hsieh ◽  
Michael J Calcutt ◽  
Linda F Chapman ◽  
Moonmoon Mitra ◽  
Daniel S Smith
Keyword(s):  
Clostridium Perfringens ◽  
Purification And Characterization

scholarly journals PURIFICATION AND CHARACTERIZATION OF ^|^alpha;-TOXIN OF CLOSTRIDIUM OEDEMATIENS TYPE A

1983 ◽  
Vol 36 (3) ◽  
pp. 135-145 ◽  
Author(s):  
NANAE IZUMI ◽  
HISASHI KONDO ◽  
IWAO OHISHI ◽  
GENJI SAKAGUCHI
Keyword(s):  
Type A ◽  
Alpha Toxin ◽  
Purification And Characterization

Purification and Characterization of α-N-Acetylgalactosaminidase from Clostridium perfringens

IUBMB Life ◽  
2000 ◽  
Vol 50 (2) ◽  
pp. 91-97
Author(s):  
Hsin-Yeh Hsieh ◽  
Moonmoon Mitra ◽  
Donald Charles Wells ◽  
Daniel Smith
Keyword(s):  
Clostridium Perfringens ◽  
Purification And Characterization

scholarly journals Characterization of Acp, a Peptidoglycan Hydrolase of Clostridium perfringens with N-Acetylglucosaminidase Activity That Is Implicated in Cell Separation and Stress-Induced Autolysis

2010 ◽  
Vol 192 (9) ◽  
pp. 2373-2384 ◽  
Author(s):  
Emilie Camiade ◽  
Johann Peltier ◽  
Ingrid Bourgeois ◽  
Evelyne Couture-Tosi ◽  
Pascal Courtin ◽  
...  
Keyword(s):  
Mutant Strain ◽  
Clostridium Perfringens ◽  
Vegetative Growth ◽  
Cell Separation ◽  
Catalytic Domain ◽  
Peptidoglycan Hydrolase ◽  
Wild Type ◽  
Induced Autolysis

ABSTRACT This work reports the characterization of the first known peptidoglycan hydrolase (Acp) produced mainly during vegetative growth of Clostridium perfringens. Acp has a modular structure with three domains: a signal peptide domain, an N-terminal domain with repeated sequences, and a C-terminal catalytic domain. The purified recombinant catalytic domain of Acp displayed lytic activity on the cell walls of several Gram-positive bacterial species. Its hydrolytic specificity was established by analyzing the Bacillus subtilis peptidoglycan digestion products by coupling reverse phase-high-pressure liquid chromatography (RP-HPLC) and matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) analysis, which displayed an N-acetylglucosaminidase activity. The study of acp expression showed a constant expression during growth, which suggested an important role of Acp in growth of C. perfringens. Furthermore, cell fractionation and indirect immunofluorescence staining using anti-Acp antibodies revealed that Acp is located at the septal peptidoglycan of vegetative cells during exponential growth phase, indicating a role in cell separation or division of C. perfringens. A knockout acp mutant strain was obtained by using the insertion of mobile group II intron strategy (ClosTron). The microscopic examination indicated a lack of vegetative cell separation in the acp mutant strain, as well as the wild-type strain incubated with anti-Acp antibodies, demonstrating the critical role of Acp in cell separation. The comparative responses of wild-type and acp mutant strains to stresses induced by Triton X-100, bile salts, and vancomycin revealed an implication of Acp in autolysis induced by these stresses. Overall, Acp appears as a major cell wall N-acetylglucosaminidase implicated in both vegetative growth and stress-induced autolysis.

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