Mechanism of actions of Oncocin, a prolinerich antimicrobial peptide, in early elongation revealed by single-molecule FRET

References

[1] Gagnon MG, Roy RN, Lomakin IB, Florin T, Mankin AS, Steitz TA (2016) Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition. Nucleic Acids Res 44:2439–2450.

[2] Geggier P, Dave R, Feldman MB, Terry DS, Altman RB, Munro JB, Blanchard SC (2010) Conformational sampling of aminoacyltRNA during selection on the bacterial ribosome. J Mol Biol 399:576–595.

[3] Hansen A, Schafer I, Knappe D, Seibel P, Hoffmann R (2012) Intracellular toxicity of proline-rich antimicrobial peptides shuttled into mammalian cells by the cell-penetrating peptide penetratin. Antimicrobial agents and chemotherapy 56:5194–5201.

[4] Johansson M, Bouakaz E, Lovmar M, Ehrenberg M (2008) The kinetics of ribosomal peptidyl transfer revisited. Mol Cell 30:589–598.

[5] Knappe D, Piantavigna S, Hansen A, Mechler A, Binas A, Nolte O, Martin LL, Hoffmann R (2010) Oncocin (VDKPPYLPRPRPPRRIYNR-NH2): a novel antibacterial peptide optimized against gram-negative human pathogens. Journal of medicinal chemistry 53:5240–5247.

[6] Knappe D, Kabankov N, Hoffmann R (2011) Bactericidal oncocin derivatives with superior serum stabilities. International journal of antimicrobial agents 37:166–170.

[7] Mattiuzzo M, Bandiera A, Gennaro R, Benincasa M, Pacor S, Antcheva N, Scocchi M (2007) Role of the Escherichia coli SbmA in the antimicrobial activity of proline-rich peptides. Mol Microbiol 66:151–163.

[8] Pan DL, Kirillov SV, Cooperman BS (2007) Kinetically competent intermediates in the translocation step of protein synthesis. Mol Cell 25:519–529

[9] Pape T, Wintermeyer W, Rodnina MV (1998) Complete kinetic mechanism of elongation factor Tu-dependent binding of aminoacyl-tRNA to the A site of the E. coli ribosome. Embo J 17:7490–7497.

[10] Peng S, Sun R, Wang W, Chen C (2017) Single-Molecule Photoactivation FRET: A General and Easy-To-Implement Approach To Break the Concentration Barrier. Angewandte Chemie 56:6882–6885.

[11] Rodnina MV, Wintermeyer W (2001) Fidelity of aminoacyl-tRNA selection on the ribosome: kinetic and structural mechanisms. Annu Rev Biochem 70:415–435.

[12] Roy RN, Lomakin IB, Gagnon MG, Steitz TA (2015) The mechanism of inhibition of protein synthesis by the proline-rich peptide oncocin. Nat Struct Mol Biol 22:466–469.

[13] Schmidt R, Ostorhazi E, Wende E, Knappe D, Hoffmann R (2016) Pharmacokinetics and in vivo efficacy of optimized oncocin derivatives. The Journal of antimicrobial chemotherapy 71:1003–1011.

[14] Seefeldt AC, Nguyen F, Antunes S, Perebaskine N, Graf M, Arenz S, Inampudi KK, Douat C, Guichard G, Wilson DN (2015) The proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complex. Nat Struct Mol Biol 22:470–475.

[15] Tomasinsig L, Skerlavaj B, Papo N, Giabbai B, Shai Y, Zanetti M (2006) Mechanistic and functional studies of the interaction of a proline-rich antimicrobial peptide with mammalian cells. J Biol Chem 281:383–391.

RIGHTS & PERMISSIONS

The Author(s) 2017. This article is an open access publication