Disease relevance of Neomycin A

• Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. II. Localization of the amino acid replacement in protein S17 from a meaA mutant [1].
• Attachment of the neamine core allows cellular uptake of the PNA and results in potent inhibition of HIV-1 replication [2].
• A mixture of these two forms of neamine was converted by deoxystreptamine-negative Streptomyces rimosus forma paromomycinus into neomycin (not paromomycin) with a 30% yield [3].
• None of the compounds exhibited better in vitro antibacterial activity than neamine when compared against Gram-positive and Gram-negative bacteria [4].
• Selectively guanidinylated derivatives of neamine. Syntheses and inhibition of anthrax lethal factor protease [5].

High impact information on Neomycin A

• Immunohistochemical staining showed that both angiogenesis and cancer cell proliferation are inhibited by neamine [6].
• Neomycin, paromomycin, ribostamycin and neamine bind in the major groove of the A-site RNA in a unique binding pocket formed by non-canonical base pairs and a bulged nucleotide [7].
• Alteration of ribosomal protein S17 by mutation linked to neamine resistance in Escherichia coli. I. General properties of neaA mutants [8].
• Aminoglycoside antibiotics that bind to the aminoacyl-tRNA site (A site) of the ribosome are composed of a common neamine core in which a glycopyranosyl ring is attached to position 4 of a 2-deoxystreptamine moiety [9].
• Quench-flow pre-steady-state kinetic analyses of the reactions of Gram-negative APH(3') types Ia and IIa with kanamycin A, neamine, and their respective difluorinated analogues 4'-deoxy-4',4'-difluorokanamycin A and 4'-deoxy-4',4'-difluoroneamine were carried out, in conjunction with measurements of thio effect and viscosity studies [10].

Chemical compound and disease context of Neomycin A

• Three different changes within a conserved region of the 16S gene, equivalent to E. coli bases 1191-1193, confer varying levels of spectinomycin resistance, while resistance to neamine and kanamycin results from mutations in the 16S gene at bases equivalent to E. coli 1408 and 1409 [11].

Biological context of Neomycin A

• Genetic and biochemical analyses indicate that the neamine-resistant phenotype is the result of two distinct mutations [12].
• It is concluded that the added neamine is incorporated into antibiotic intact, without initial hydrolysis, and that the probable first step in the subunit assembly of neomycin is the formation of neamine [3].
• Regioselective glycosylation of neamine core: a facile entry to kanamycin B related analogues [13].
• The use of neamine as a molecular template: inactivation of bacterial antibiotic resistance enzyme aminoglycoside 3'-phosphotransferase type IIa [14].
• In the search for antiviral agents targeting multiple binding sites for aminoglycosides in RNA, we report here the synthesis of new neamine dimers and a trimer in which the neamine cores are connected by different linking chains attached at the 4'- and/or 5-positions [15].

Anatomical context of Neomycin A

• RESULTS: Neamine effectively blocked the nuclear translocation of angiogenin in endothelial cells and inhibited angiogenin-induced cell proliferation [6].

Associations of Neomycin A with other chemical compounds

• By this technique commercial neomycin complex, neamine (neomycin A), neomycin B, neomycin C, and streptomycin were found to be allergenic in guinea pigs via intradermal (id) and foot-pad (fp) immunizations [16].

Gene context of Neomycin A

• The neamine part of the aminoglycoside antibiotic neomycin B was conjugated to a 16 mer peptide nucleic acid (PNA) targeting HIV-1 TAR RNA [2].
• Chemical modification of neamine. Part III [17].

Analytical, diagnostic and therapeutic context of Neomycin A

• The antitumor activity of neamine was determined with three different animal models [6].
• EXPERIMENTAL DESIGN: The effect of neamine on the nuclear translocation of angiogenin was examined by means of immunofluorescence and Western blotting [6].
• Gradient elution and isocratic HPLC methods for the analysis of derivatized neamine have also been developed [18].

References