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Updated: May 9, 2026

Antimicrobial Peptides Produced by Selective Pressure Incorporation of Non-canonical Amino Acids
Published on: May 4, 2018
New type of antimicrobial protein produced by the plant pathogen Clavibacter michiganensis subsp. michiganensis
Zhanliang Liu1, Ping Ma, Ingrid Holtsmark
1Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.
Abstract:
It has previously been shown that the tomato pathogen Clavibacter michiganensis subsp. michiganensis secretes a 14-kDa protein, C. michiganensis subsp. michiganensis AMP-I (CmmAMP-I), that inhibits growth of Clavibacter michiganensis subsp. sepedonicus, the causal agent of bacterial ring rot of potato. Using sequences obtained from tryptic fragments, we have identified the gene encoding CmmAMP-I and we have recombinantly produced the protein with an N-terminal intein tag. The gene sequence showed that CmmAMP-I contains a typical N-terminal signal peptide for Sec-dependent secretion. The recombinant protein was highly active, with 50% growth inhibition (IC50) of approximately 10 pmol, but was not toxic to potato leaves or tubers. CmmAMP-I does not resemble any known protein and thus represents a completely new type of bacteriocin. Due to its high antimicrobial activity and its very narrow inhibitory spectrum, CmmAMP-1 may be of interest in combating potato ring rot disease.
Insights
A novel protein, Clavibacter michiganensis subsp. michiganensis AMP-I (CmmAMP-I), inhibits potato ring rot bacteria. This newly identified bacteriocin shows high activity and may combat the disease effectively.
Area of Science:
- Plant Pathology
- Bacteriology
- Biochemistry
Background:
- Clavibacter michiganensis subsp. michiganensis (Cmm) produces a protein inhibiting Clavibacter michiganensis subsp. sepedonicus (Cms).
- Cms causes bacterial ring rot, a significant potato disease.
Purpose of the Study:
- Identify the gene encoding the Cmm-secreted inhibitory protein, CmmAMP-I.
- Recombinantly produce and characterize CmmAMP-I for its antimicrobial properties and potential applications.
Main Methods:
- Gene identification using tryptic fragment sequences.
- Recombinant protein production with an N-terminal intein tag.
- Antimicrobial activity assays to determine IC50 and toxicity.
Main Results:
- The gene encoding CmmAMP-I was identified, revealing a Sec-dependent signal peptide.
- Recombinant CmmAMP-I exhibited high antimicrobial activity (IC50 ~10 pmol).
- The protein showed no toxicity to potato tissues and represents a novel bacteriocin class.
Conclusions:
- CmmAMP-I is a new type of bacteriocin with potent activity against Cms.
- Its narrow spectrum and lack of phytotoxicity make it a promising candidate for controlling potato bacterial ring rot.
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