Blasticidin S

Blasticidin S is a peptidyl nucleoside produced by several species of Streptomyces that was first isolated from S. griseochromogenes in 1958. Blasticidin S inhibits protein synthesis and is active against bacteria, fungi, nematodes, and tumor cells. The compound is used as a selection antibiotic for both eukaryotic and prokaryotic cells, and a marker for strain manipulation. It can be used in genome editing using the CRISPR/Cas9 system.
Blasticidin S is soluble in water, methanol, DMF or DMSO.

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Background

Blasticidin S inhibits protein synthesis in prokaryotic and eukaryotic cells by binding to the ribosomal P-site which strengthens tRNA binding and slows down and prevents subsequent peptide synthesis.
Mechanisms of resistance
Resistance to Blasticidin S is conferred by bsr, bsd, and bls resistance genes isolated from Bacillus cereus K55-S1, Aspergillus terreus, and Streptoverticillum spp, respectively.
The bsr resistance gene is a 420 bp fragment and encodes a 15 kDa Blasticidin S deaminase which catalyzes the reaction of Blasticidin S to deaminohydroxyblasticidin S. Deaminohydroxyblasticidin S is a biologically inactive derivative of Blasticidin S and does not interact with or inhibit prokaryotic or eukaryotic ribosomes.
The bsd resistance gene is a 393 bp fragment and also encodes a Blasticidin S deaminase enzyme which catalyzes a similar reaction to the BSR deaminase. A study by Kimura et al. found the transfection frequency with bsd to be 80X greater than with bsr when using FM3A cells.
The bls gene resistance gene encodes an acetyltransferase which interacts with acetyl-coenzyme A and prevents Blasticidin S from inhibiting protein synthesis.