Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides
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Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides. / Mattiuzzo, Maura; De Gobba, Cristian; Runti, Giulia; Mardirossian, Mario; Bandiera, Antonella; Gennaro, Renato; Scocchi, Marco.
In: Journal of Microbiology and Biotechnology, Vol. 24, No. 2, 2014, p. 160-167.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Proteolytic activity of Escherichia coli oligopeptidase B against proline-rich antimicrobial peptides
AU - Mattiuzzo, Maura
AU - De Gobba, Cristian
AU - Runti, Giulia
AU - Mardirossian, Mario
AU - Bandiera, Antonella
AU - Gennaro, Renato
AU - Scocchi, Marco
PY - 2014
Y1 - 2014
N2 - Oligopeptidase B (OpdB) is a serine peptidase widespread among bacteria and protozoa that has emerged as a virulence factor despite its function has not yet been precisely established. By using an OpdB-overexpressing Escherichia coli strain, we found that the overexpressed peptidase makes the bacterial cells specifically less susceptible to several proline-rich antimicrobial peptides known to penetrate into the bacterial cytosol, and that its level of activity directly correlates with the degree of resistance. We established that E. coli OpdB can efficiently hydrolyze in vitro cationic antimicrobial peptides up to 30 residues in length, even though they contained several prolines, shortening them to inactive fragments. Two consecutive basic residues are a preferred cleavage site for the peptidase. In the case of a single basic residue, there is no cleavage if proline residues are present in the P1 and P2 positions. These results also indicate that cytosolic peptidases may cause resistance to antimicrobial peptides that have an intracellular mechanism of action, such as the proline-rich peptides, and may contribute to define the substrate specificity of the E. coli OpdB.
AB - Oligopeptidase B (OpdB) is a serine peptidase widespread among bacteria and protozoa that has emerged as a virulence factor despite its function has not yet been precisely established. By using an OpdB-overexpressing Escherichia coli strain, we found that the overexpressed peptidase makes the bacterial cells specifically less susceptible to several proline-rich antimicrobial peptides known to penetrate into the bacterial cytosol, and that its level of activity directly correlates with the degree of resistance. We established that E. coli OpdB can efficiently hydrolyze in vitro cationic antimicrobial peptides up to 30 residues in length, even though they contained several prolines, shortening them to inactive fragments. Two consecutive basic residues are a preferred cleavage site for the peptidase. In the case of a single basic residue, there is no cleavage if proline residues are present in the P1 and P2 positions. These results also indicate that cytosolic peptidases may cause resistance to antimicrobial peptides that have an intracellular mechanism of action, such as the proline-rich peptides, and may contribute to define the substrate specificity of the E. coli OpdB.
KW - Antimicrobial peptide
KW - proline-rich
KW - oligopeptidase B
KW - proteolysis
U2 - 10.4014/jmb.1310.10015
DO - 10.4014/jmb.1310.10015
M3 - Journal article
VL - 24
SP - 160
EP - 167
JO - Microbiology and Biotechnology Letters
JF - Microbiology and Biotechnology Letters
SN - 1598-642X
IS - 2
ER -
ID: 124770654