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Function of Penicillin-binding protein 3 in Streptococcus Faecium
Coyette, Jacques; Somzé, Anne; Briquet, Jean-Jacques et al.
1983In Hakenbeck, Regine; Höltje, Joachim-Volker; Labischinski, Harald (Eds.) The Target Penicillin : the Murein Sacculus of Bacterial Cell Walls Architecture and Growth : Proceedings
 

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Keywords :
Streptococcus faecium; penicillin-binding proteins; penicillin
Abstract :
[en] Cefotaxime at concns. around the min. inhibitory concn. (MIC, 5 μM) or below (0.1-1.0 μM) causes transformation of the normal S. faecium cells to bacilliform cells whose length increases with increasing duration of treatment. Septa are initiated but never reach completion. Affinity detn. for cefotaxime binding showed that the antibiotic binds preferentially to the 3 highest mol. wt. penicillin-binding proteins (PBP); PBP-2 and PBP-3 are about 100-fold more sensitive to cefotaxime than PBP-1. It appears, therefore, that PbP-2 and PBP-3 are involved in cell septation. This was confirmed by using cefatoxime in subinhibitory concns. (1 μM). From cell samples collected 30 and 60 min after addn. of cefotaxime, membranes were isolated, labeled with satg. [3H]benzylpenicillin and examd. by fluorog. Under these conditions only PBP-2 and PBP-3 were satd. by cefotaxime. At this stage no distinction could be made between the 2 proteins; either both or 1 of them may be involved in cell division. Cefoxitin produced morphol. alteration of a different nature than cefotaxime. The cefoxitin-treated cells had increased diam. and were slightly elongated. The most striking alteration was the frequent presence of conical poles contrasting with round poles obsd. in control cells. The morphol. alteration obsd. in cefoxitin-treated cells could be attributed to the inhibition of the function of PBP-1, PBP-2, or PBP-3. Elongated cells similar to those obtained with cefotaxime were not found with cefoxitin at concns. sufficient to sat. PBP-2. The main difference between cefotaxime- and cefoxitin-treated cells is that PBP-3 is satd. by cefotaxime but not altered at all by cefoxitin. Thus, septation inhibition must be due to the interaction of cefotaxime with PBP-3
Disciplines :
Biochemistry, biophysics & molecular biology
Microbiology
Author, co-author :
Coyette, Jacques;  Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie
Somzé, Anne;  Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie
Briquet, Jean-Jacques;  Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie
Ghuysen, Jean-Marie ;  Université de Liège - ULiège > Faculté de Médecine, Institut de Chimie > Service de Microbiologie
Fontana, Roberta;  Università degli Studi di Padova > Istituto di microbiologia
Language :
English
Title :
Function of Penicillin-binding protein 3 in Streptococcus Faecium
Publication date :
1983
Event name :
International FEMS Symposium
Event place :
Berlin (West), Germany
Event date :
March 13-18
Audience :
International
Main work title :
The Target Penicillin : the Murein Sacculus of Bacterial Cell Walls Architecture and Growth : Proceedings
Editor :
Hakenbeck, Regine
Höltje, Joachim-Volker
Labischinski, Harald
Publisher :
Walter de Gruyter & Co
ISBN/EAN :
3110097052
978-3110097054
Pages :
523-529
Available on ORBi :
since 26 May 2011

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