Abstract
The effects of variations in growth conditions on the penicillin response of Streptococcus faecium ATCC 9790 were studied. Changes in the growth temperature and medium composition were found to cause striking changes in the bacterial generation time, cellular penicillin sensitivity (minimum inhibitory concentration), sensitivity of peptidoglycan synthesis to inhibition by penicillin, rate of autolysis, and labeling pattern of penicillin-binding proteins. However, no constant relationship between these parameters and the minimum inhibitory concentration could be observed. Similar electrophoretic patterns for penicillin-binding proteins were observed in cells grown in different media at the optimal growth temperature. Inhibition of cell division by penicillin in cells grown at this temperature (but not at higher or lower temperatures) caused filamentation of the bacteria. In cells grown in a chemically defined medium at the optimal temperature (but not at temperatures above or below), complete inhibition of cell division was associated with only partial inhibition (34% after 150 min) of peptidoglycan synthesis. It is suggested that the status and physiological importance of individual penicillin-binding proteins in S. faecium are heavily influenced by growth conditions. Depending on the growth conditions, different penicillin-binding proteins may perform the cellular function, indispensible for bacterial growth.
MeSH Terms
Bacterial Proteins
Bacteriolysis
Carrier Proteins/metabolism
Cell Division/drug effects
Culture Media
Dose-Response Relationship, Drug
Hexosyltransferases
Muramoylpentapeptide Carboxypeptidase
Penicillin G/pharmacology
Penicillin-Binding Proteins
Peptidoglycan/biosynthesis
Peptidyl Transferases
Streptococcus/cytology,drug effects,physiology
Temperature
Chemicals
Bacterial Proteins
Carrier Proteins
Culture Media
Penicillin-Binding Proteins
Peptidoglycan
Peptidyl Transferases
Hexosyltransferases
Muramoylpentapeptide Carboxypeptidase
Penicillin G
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Fontana R
Canepari P
Satta G
Coyette J
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20 references, click to expand
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