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

Abstract 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...

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Autores principales: M. Aftab Uddin, Shammi Akter, Mahbuba Ferdous, Badrul Haidar, Al Amin, A. H. M. Shofiul Islam Molla, Haseena Khan, Mohammad Riazul Islam
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Publicado: Nature Portfolio 2021
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spelling oai:doaj.org-article:e760517fbe364ade8b62996084b434ef2021-12-02T15:49:35ZA plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant10.1038/s41598-021-90613-92045-2322https://doaj.org/article/e760517fbe364ade8b62996084b434ef2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-90613-9https://doaj.org/toc/2045-2322Abstract 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.M. Aftab UddinShammi AkterMahbuba FerdousBadrul HaidarAl AminA. H. M. Shofiul Islam MollaHaseena KhanMohammad Riazul IslamNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Medicine
R
Science
Q
spellingShingle Medicine
R
Science
Q
M. Aftab Uddin
Shammi Akter
Mahbuba Ferdous
Badrul Haidar
Al Amin
A. H. M. Shofiul Islam Molla
Haseena Khan
Mohammad Riazul Islam
A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant
description Abstract 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.
format article
author M. Aftab Uddin
Shammi Akter
Mahbuba Ferdous
Badrul Haidar
Al Amin
A. H. M. Shofiul Islam Molla
Haseena Khan
Mohammad Riazul Islam
author_facet M. Aftab Uddin
Shammi Akter
Mahbuba Ferdous
Badrul Haidar
Al Amin
A. H. M. Shofiul Islam Molla
Haseena Khan
Mohammad Riazul Islam
author_sort M. Aftab Uddin
title A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant
title_short A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant
title_full A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant
title_fullStr A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant
title_full_unstemmed A plant endophyte Staphylococcus hominis strain MBL_AB63 produces a novel lantibiotic, homicorcin and a position one variant
title_sort plant endophyte staphylococcus hominis strain mbl_ab63 produces a novel lantibiotic, homicorcin and a position one variant
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/e760517fbe364ade8b62996084b434ef
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