Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2003 Jul;16(3):430-50.
doi: 10.1128/CMR.16.3.430-450.2003.

Versatility of aminoglycosides and prospects for their future

Sergei B Vakulenko  1 , Shahriar Mobashery
Affiliations
Review

Versatility of aminoglycosides and prospects for their future

Sergei B Vakulenko et al. Clin Microbiol Rev. 2003 Jul.

Abstract

Aminoglycoside antibiotics have had a major impact on our ability to treat bacterial infections for the past half century. Whereas the interest in these versatile antibiotics continues to be high, their clinical utility has been compromised by widespread instances of resistance. The multitude of mechanisms of resistance is disconcerting but also illuminates how nature can manifest resistance when bacteria are confronted by antibiotics. This article reviews the most recent knowledge about the mechanisms of aminoglycoside action and the mechanisms of resistance to these antibiotics.

PubMed Disclaimer

Figures

FIG. 1.
FIG. 1.
Sites of modification by aminoglycoside-modifying enzymes.
FIG. 2.
FIG. 2.
Phosphorylation of kanamycin A by APH(3′)s.
FIG. 3.
FIG. 3.
Acetylation of kanamycin A by AAC(6′)s.
FIG. 4.
FIG. 4.
Adenylation of kanamycin A by ANT(2").
FIG. 5.
FIG. 5.
Mechanism-based inhibition of APH(3′)s.
FIG. 6.
FIG. 6.
Cyclic process of phosphorylation and release of inorganic phosphate for derivative 5 of kanamycin A.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Ainsa, J. A., C. Martin, B. Gicquel, and R. Gomez-Lus. 1996. Characterization of the chromosomal aminoglycoside 2′-N-acetyltransferase gene from Mycobacterium fortuitum. Antimicrob. Agents Chemother. 40:2350-2355. - PMC - PubMed
    1. Ainsa, J. A., E. Perez, V. Pelicic, F. X. Berthet, B. Gicquel, and C. Martin. 1997. Aminoglycoside 2′-N-acetyltransferase genes are universally present in mycobacteria: characterization of the aac(2′)-Ic gene from Mycobacterium tuberculosis and the aac(2′)-Id gene from Mycobacterium smegmatis. Mol. Microbiol. 24:431-441. - PubMed
    1. Aires, J. R., T. Kohler, H. Nikaido, and P. Plesiat. 1999. Involvement of an active efflux system in the natural resistance of Pseudomonas aeruginosa to aminoglycosides. Antimicrob. Agents Chemother. 43:2624-2628. - PMC - PubMed
    1. Akova, M., D. Gur, D. M. Livermore, T. Kocagoz, and H. E. Akalin. 1999. In vitro activities of antibiotics alone and in combination against Brucella melitensis at neutral and acidic pHs. Antimicrob. Agents Chemother. 43:1298-1300. - PMC - PubMed
    1. Allmansberger, R., B. Brau, and W. Piepersberg. 1985. Genes for gentamicin-(3)-N-acetyl-transferases III and IV. II. Nucleotide sequences of three AAC(3)-III genes and evolutionary aspects. Mol. Gen. Genet. 198:514-520. - PubMed

MeSH terms

Substances