JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Miller, M A
Right arrow Articles by Mills, J
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Miller, M A
Right arrow Articles by Mills, J

 Previous Article  |  Next Article 

J Bacteriol. 1980 July; 143(1): 198-204

Cytoplasmic membrane proteins of spectinomycin-susceptible and -resistant strains of Neisseria gonorrhoeae.

M A Miller, C S Schärli and J Mills

ABSTRACT

Cytoplasmic membranes were isolated and examined from two spectinomycin-susceptible and three spectinomycin-resistant clinical strains of Neisseria gonorrhoeae. A laboratory-derived spectinomycin-resistant mutant, obtained by serial passage on gradually increasing concentrations of the antibiotic, and a susceptible revertant, spontaneously arising from one of the resistant clinical strains, were also studied. Sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis revealed that a major protein, comprising about 7% of total cytoplasmic membrane protein (molecular weight 24,000), was absent in the three clinically isolated spectinomycin-resistant strains. In a revertant, this protein reappeared. During treatment of one of the susceptible strains with spectinomycin, the protein disappeared. However, this correlation was not maintained in the laboratory-derived spectinomycin-resistant mutant. This mutant was of comparable resistant to the clinical isolates, but the 24,000-molecular-weight protein was present in normal quantities. In addition, spectinomycin resistant in clinical isolates was variable compared with stable resistance exhibited by the laboratory-derived mutant. These findings suggested that differences in laboratory-derived versus clinical spectinomycin resistance may be due to different types of resistance mutations.

J Bacteriol. 1980 July; 143(1): 198-204






Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 1980 by the American Society for Microbiology. All rights reserved.