Isolation, Identification, and Bioinformatic Analysis of Antibacterial Proteins and Peptides from Immunized Hemolymph of Red Palm Weevil Rhynchophorus ferrugineus

• Published in: Biomolecules (Basel, Switzerland) Vol. 11; no. 1; p. 83
• Main Authors: Knutelski, Stanisław, Awad, Mona, Łukasz, Natalia, Bukowski, Michał, Śmiałek, Justyna, Suder, Piotr, Dubin, Grzegorz, Mak, Paweł
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 11.01.2021; MDPI
• Subjects: Adults; Antimicrobial agents; antimicrobial proteins/peptides; attacins; Bacteria; Cecropin; cecropins; Contemporary problems; Defensins; Drug resistance; E coli; Gene expression; Gram-negative bacteria; Gram-positive bacteria; Hemolymph; High-performance liquid chromatography; Insects; Isoforms; Mass spectroscopy; Peptides; pheromone-binding proteins; Proteins; Rhynchophorus ferrugineus; Transcriptomes; United States > US; defensins; cecropins; antimicrobial proteins/peptides; attacins; bioinformatics; pheromone-binding proteins; Rhynchophorus ferrugineus; odorant-binding proteins
• ISSN: 2218-273X; 2218-273X
• DOI: 10.3390/biom11010083

Red palm weevil ( Olivier, 1791, Coleoptera: Curculionidae) is a destructive pest of palms, rapidly extending its native geographical range and causing large economic losses worldwide. The present work describes isolation, identification, and bioinformatic analysis of antibacterial proteins and peptides from the immunized hemolymph of this beetle. In total, 17 different bactericidal or bacteriostatic compounds were isolated via a series of high-pressure liquid chromatography steps, and their partial amino acid sequences were determined by N-terminal sequencing or by mass spectrometry. The bioinformatic analysis of the results facilitated identification and description of corresponding nucleotide coding sequences for each peptide and protein, based on the recently published transcriptome database. The identified compounds are represented by several well-known bactericidal factors: two peptides similar to defensins, one cecropin-A1-like peptide, and one attacin-B-like protein. Interestingly, we have also identified some unexpected compounds comprising five isoforms of pheromone-binding proteins as well as seven isoforms of odorant-binding proteins. The particular role of these factors in insect response to bacterial infection needs further investigation.