A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant

• Published in: Scientific reports Vol. 11; no. 1; p. 11211
• Main Authors: Aftab Uddin, M., Akter, Shammi, Ferdous, Mahbuba, Haidar, Badrul, Amin, Al, Shofiul Islam Molla, A. H. M., Khan, Haseena, Islam, Mohammad Riazul
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 27.05.2021; Nature Portfolio
• Subjects: 631/154; 631/326; Bacteriocins - analysis; Endophytes - chemistry; Endophytes - metabolism; Humanities and Social Sciences; Mass Spectrometry; multidisciplinary; Science; Science (multidisciplinary); Staphylococcus hominis - chemistry; Staphylococcus hominis - metabolism
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/s41598-021-90613-9

Here we report a jute endophyte Staphylococcus hominis strain MBL_AB63 isolated from jute seeds which showed promising antimicrobial activity against Staphylococcus aureus SG511 when screening for antimicrobial substances. The whole genome sequence of this strain, annotated using BAGEL4 and antiSMASH 5.0 to predict the gene clusters for antimicrobial substances identified a novel antimicrobial peptide cluster that belongs to the class I lantibiotic group. The predicted lantibiotic (homicorcin) was found to be 82% similar to a reported peptide epicidin 280 having a difference of seven amino acids at several positions of the core peptide. Two distinct peaks obtained at close retention times from a RP-HPLC purified fraction have comparable antimicrobial activities and LC–MS revealed the molecular mass of these peaks to be 3046.5 and 3043.2 Da. The presence of an oxidoreductase ( homO ) similar to that of epicidin 280- associated eciO or epilancin 15X- associated elxO in the homicorcin gene cluster is predicted to be responsible for the reduction of the first dehydrated residue dehydroalanine (Dha) to 2-hydroxypropionate that causes an increase of 3 Da mass of homicorcin 1. Trypsin digestion of the core peptide and its variant followed by ESI–MS analysis suggests the presence of three ring structures, one in the N-terminal and other two interlocking rings at the C-terminal region that remain undigested. Homicorcin exerts bactericidal activity against susceptible cells by disrupting the integrity of the cytoplasmic membrane through pore formation as observed under FE-SEM.