RRC ID 59059
Author Uchi N, Fukudome M, Nozaki N, Suzuki M, Osuki KI, Shigenobu S, Uchiumi T.
Title Antimicrobial Activities of Cysteine-rich Peptides Specific to Bacteriocytes of the Pea Aphid Acyrthosiphon pisum.
Journal Microbes Environ.
Abstract Aphids have a mutualistic relationship with the bacterial endosymbiont Buchnera aphidicola. We previously reported seven cysteine-rich peptides in the pea aphid Acyrthosiphon pisum and named them Bacteriocyte-specific Cysteine-Rich (BCR) peptides; these peptides are exclusively expressed in bacteriocytes, special aphid cells that harbor symbionts. Similar symbiotic organ-specific cysteine-rich peptides identified in the root nodules of leguminous plants are named Nodule-specific Cysteine-Rich (NCR) peptides. NCR peptides target rhizobia in the nodules and are essential for symbiotic nitrogen fixation. A BacA (membrane protein) mutant of Sinorhizobium is sensitive to NCR peptides and is unable to establish symbiosis. Based on the structural and expressional similarities between BCR peptides and NCR peptides, we hypothesized that aphid BCR peptides exhibit antimicrobial activity, similar to some NCR peptides. We herein synthesized BCR peptides and investigated their antimicrobial activities and effects on the bacterial membrane of Escherichia coli. The peptides BCR1, BCR3, BCR5, and BCR8 exhibited antimicrobial activities with increased membrane permeability. An sbmA mutant of E. coli, a homolog of bacA of S. meliloti, was more sensitive to BCR peptides than the wild type. Our results suggest that BCR peptides have properties that may be required to control the endosymbiont, similar to NCR peptides in legumes.
Volume 34(2)
Pages 155-160
Published 2019-6-27
DOI 10.1264/jsme2.ME18148
PMID 30905896
PMC PMC6594739
MeSH Animals Anti-Infective Agents / chemical synthesis Anti-Infective Agents / chemistry Anti-Infective Agents / pharmacology* Aphids / metabolism* Aphids / microbiology Buchnera / physiology Cell Membrane Permeability / drug effects Cell Membrane Permeability / genetics Cysteine / chemistry* Escherichia coli / cytology Escherichia coli / drug effects Escherichia coli / genetics Insect Proteins / chemical synthesis Insect Proteins / chemistry Insect Proteins / pharmacology* Mutation Peptides / chemical synthesis Peptides / chemistry Peptides / pharmacology* Sinorhizobium meliloti / drug effects Sinorhizobium meliloti / genetics Symbiosis
IF 2.575
Times Cited 1
Prokaryotes E. coli JW0368