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PMID: 2877048 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Mutants of Streptococcus pneumoniae that contain a temperature-sensitive autolysin.

Journal of general microbiology ·Vol. 132 ·No. 5 ·1986-05-00 ·Pages 1401-5

García P, García E, Ronda C, Lopez R, Jiang RZ, Tomasz A

Abstract

Two mutants of Streptococcus pneumoniae deficient in autolysin activity produced a protein that showed immunological identity with the N-acetyl-muramyl-L-alanyl-amidase present in the wild-type strain, when tested with antiserum obtained against this enzyme. The protein was produced by the mutant cultures grown either at 37 degrees C or at 30 degrees C, although only the cell extracts obtained at 30 degrees C showed significant cell wall hydrolysing activity. In contrast to the lysis resistance of these bacteria grown at 37 degrees C, mutant cultures grown at 30 degrees C exhibited significant degrees of autolysis when treated with detergent or cell wall inhibitors. Extracts of the mutant cultures contained a cell wall hydrolysing activity that was rapidly inactivated during incubation at 37 degrees C.

MeSH Terms
Amidohydrolases/analysis Bacteriolysis Immunodiffusion Mutation N-Acetylmuramoyl-L-alanine Amidase/analysis Penicillin G/metabolism Streptococcus pneumoniae/analysis,genetics,metabolism Temperature
Chemicals
Amidohydrolases N-Acetylmuramoyl-L-alanine Amidase Penicillin G
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
García P
García E
Ronda C
Lopez R
Jiang R Z
Tomasz A
Article Info
Journal
Journal of general microbiology
Abbr.
J Gen Microbiol
ISSN
0022-1287
Published
1986-05-00
Pages
1401-5
Language
English
Region
England
NLM ID
0375371
Subset
IM
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