Abstract

Streptococcus faecium possess two Beta,1-4 N-acetylmuramidases (MUR1 and MUR2) which degrade peptidoglycan with different specifities. Furthermore, MUR1 can be found in a latent and proteolytically activated form. Penicillin-tolerant derivatives have been obtained containing substantially reduced levels of activated MUR1, and increased levels of activated MUR2. Possible models for the regulation of these enzymes will be tested. Various penicillin-tolerant and -sensitive derivatives will be obtained, characterized and compared to derivatives defective in MUR1, MUR2 or proteolytic activator functions. From these studies we should derive a better understanding of the regulation of autolytic activity in streptococci and clarify a previously proposed relationship between autolysis and antibiotic lethality.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Research Project (R01)
Project #
5R01AI023394-03
Application #
3135421
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1986-09-01
Project End
1990-08-31
Budget Start
1988-09-01
Budget End
1990-08-31
Support Year
3
Fiscal Year
1988
Total Cost
Indirect Cost

  Institution

Name
Temple University
Department
Type
Schools of Medicine
DUNS #
City
Philadelphia
State
PA
Country
United States
Zip Code
19122

  Publications

Kariyama, R; Massidda, O; Daneo-Moore, L et al. (1990) Properties of cell wall-associated DD-carboxypeptidase of Enterococcus hirae (Streptococcus faecium) ATCC 9790 extracted with alkali. J Bacteriol 172:3718-24
Dolinger, D L; Daneo-Moore, L; Shockman, G D (1989) The second peptidoglycan hydrolase of Streptococcus faecium ATCC 9790 covalently binds penicillin. J Bacteriol 171:4355-61
Said, I; Fletcher, H; Volpe, A et al. (1987) Penicillin tolerance in Streptococcus faecium ATCC 9790. Antimicrob Agents Chemother 31:1150-2