Abstract
Streptococcus pneumoniae undergoes phase variation in colony morphology, which has been implicated as a factor in the pathogenesis of pneumococcal disease. Phenotypic differences between opaque and transparent colony forms correlate with differences in rates of autolysis. This study examined whether differences in autolysis are caused by differences in expression of the major amidase, LytA, or the structure of its peptidoglycan substrate. No significant difference was detected by high-pressure liquid chromatography analysis of stem peptides released after treatment of purified peptidoglycan with amidase. Differences in the rate of digestion of purified cell walls, furthermore, did not correlate with susceptibility to autolysis. Lower levels of autolysis in opaque variants, however, was associated with decreased levels of immunodetectable LytA on colony immunoblots and Western blots (immunoblots). Diminished cell-surface-associated LytA in opaque variants was also demonstrated by whole-cell inhibition enzyme-linked immunosorbent assay. Since transparent variants have been shown both to colonize the nasopharynx more efficiently in an animal model and to express more surface-exposed LytA, it was determined whether LytA contributes to colonization in a neonatal rat model of pneumococcal carriage. Defined mutants in the lytA gene were used to show that there was no significant contribution by LytA to nasopharyngeal colonization in this model. Although the expression of LytA was shown to undergo phase variation in association with colony morphology, lytA mutants are still capable of phenotypic variation in colony morphology, which suggests that other factors are responsible for intrastrain differences which affect colonization.
MeSH Terms
Animals
Cell Wall/physiology
Enzymes/analysis,physiology
N-Acetylmuramoyl-L-alanine Amidase
Nasopharynx/microbiology
Peptidoglycan/metabolism
Rats
Streptococcus pneumoniae/physiology
Chemicals
Enzymes
Peptidoglycan
N-Acetylmuramoyl-L-alanine Amidase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Weiser J N
Department of Pediatrics, Children's Hospital of Philadelphia, Pennsylvania, USA.
Markiewicz Z
Tuomanen E I
Wani J H
References (18)
18 references, click to expand
-
Interaction of the pneumococcal amidase with lipoteichoic acid and choline.
Eur J Biochem. 1985 Jan 15;146(2):417-27
PMID: 3967665
-
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.
Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350-4
PMID: 388439
-
Teichoic acid-containing muropeptides from Streptococcus pneumoniae as substrates for the pneumococcal autolysin.
J Bacteriol. 1987 Feb;169(2):447-53
PMID: 2879828
-
Structure of the peptide network of pneumococcal peptidoglycan.
J Biol Chem. 1987 Nov 15;262(32):15400-5
PMID: 2890629
-
Overproduction and rapid purification of the amidase of Streptococcus pneumoniae.
Arch Microbiol. 1987;149(1):52-6
PMID: 3426369
-
Insertional inactivation of the major autolysin gene of Streptococcus pneumoniae.
J Bacteriol. 1988 Dec;170(12):5931-4
PMID: 2903859
-
Subcellular localization of the major pneumococcal autolysin: a peculiar mechanism of secretion in Escherichia coli.
J Biol Chem. 1989 Jan 15;264(2):1238-44
PMID: 2562954
-
Contribution of autolysin to virulence of Streptococcus pneumoniae.
Infect Immun. 1989 Aug;57(8):2324-30
PMID: 2568343
-
Protein-bound choline is released from the pneumococcal autolytic enzyme during adsorption of the enzyme to cell wall particles.
J Bacteriol. 1990 May;172(5):2241-4
PMID: 1970559
-
Role of the major pneumococcal autolysin in the atypical response of a clinical isolate of Streptococcus pneumoniae.
J Bacteriol. 1992 Sep;174(17):5508-15
PMID: 1355082
-
The cell wall mediates pneumococcal attachment to and cytopathology in human endothelial cells.
Infect Immun. 1993 Apr;61(4):1538-43
PMID: 8454360
-
Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization.
Infect Immun. 1994 Jun;62(6):2582-9
PMID: 8188381
-
Relationship between colonial morphology and adherence of Streptococcus pneumoniae.
Infect Immun. 1995 Mar;63(3):757-61
PMID: 7868244
-
Gonococcal opacity: lectin-like interactions between Opa proteins and lipooligosaccharide.
Infect Immun. 1995 Apr;63(4):1434-9
PMID: 7890406
-
Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor.
Nature. 1995 Oct 5;377(6548):435-8
PMID: 7566121
-
The genetic basis of colony opacity in Streptococcus pneumoniae: evidence for the effect of box elements on the frequency of phenotypic variation.
Mol Microbiol. 1995 Apr;16(2):215-27
PMID: 7565084
-
A study of the genetic material determining an enzyme in Pneumococcus.
Biochim Biophys Acta. 1960 Apr 22;39:508-18
PMID: 14413322
-
Involvement of a change in penicillin target and peptidoglycan structure in low-level resistance to beta-lactam antibiotics in Neisseria gonorrhoeae.
Antimicrob Agents Chemother. 1985 Jul;28(1):90-5
PMID: 3929684