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Puroindolines are small, amphipathic, wheat proteins that determine the hardness of the wheat kernel and protect crops from different pathogens. Puroindoline A (PinA) and puroindoline B (PinB) are two major isoforms of puroindolines. These proteins have antibacterial and antifungal properties mainly attributed to their characteristic tryptophan-rich domains (TRDs). In this  in vitro  study, we investigated the antimicrobial effect of PinA and PinB synthetic peptides against the growth and biofilm formation of  Campylobacter jejuni .  C. jejuni  is an important microaerobic, foodborne pathogen that causes gastrointestinal and neurological diseases in humans. Our results showed that: (1) PinA, but not PinB, has strong antimicrobial activity against  C. jejuni  clinical strains 81-176 and F38011,  Escherichia coli  O157:H7, methicillin-resistant  Staphylococcus aureus ,  Salmonella enterica  serovar Typhimurium, and  Listeria monocytogenes ; (2) The substitution of two tryptophan residues to glycine (W→G) in the TRD of PinA abolishes its antimicrobial activity against these microorganisms; (3) PinA functions additively with two common antibiotics (ciprofloxacin and erythromycin) to inhibit or inactivate  C. jejuni  strains; (4) PinA damages the  C. jejuni  cellular membrane, (5) PinA is cytotoxic to human INT 407 cells at high concentrations; and (6) PinA inhibits  C. jejuni  biofilm formation. In summary, this study demonstrates the antimicrobial activity of PinA against  C. jejuni  growth and biofilm formation and further confirms the potential use of PinA as a therapeutic agent in health care or as preservatives in the agri-food industry.

Inhibitory Effect of Puroindoline Peptides on Campylobacter jejuni Growth and Biofilm Formation