Show simple item record

dc.contributor.authorOuertani, Awatef
dc.contributor.authorChaabouni, Ines
dc.contributor.authorMosbah, Amor
dc.contributor.authorLong, Justine
dc.contributor.authorBarakat, Mohamed
dc.contributor.authorMansuelle, Pascal
dc.contributor.authorMghirbi, Olfa
dc.contributor.authorNajjari, Afef
dc.contributor.authorOuzari, Hadda-Imene
dc.contributor.authorMasmoudi, Ahmed S
dc.contributor.authorMaresca, Marc
dc.contributor.authorOrtet, Philippe
dc.contributor.authorGigmes, Didier
dc.contributor.authorMabrouk, Kamel
dc.contributor.authorCherif, Ameur
dc.date.accessioned2021-09-08T06:12:26Z
dc.date.available2021-09-08T06:12:26Z
dc.date.issued2018-06-20
dc.identifier.citationOuertani, A., Chaabouni, I., Mosbah, A., Long, J., Barakat, M., Mansuelle, P., … Cherif, A. (2018). Two New Secreted Proteases Generate a Casein-Derived Antimicrobial Peptide in Bacillus cereus Food Born Isolate Leading to Bacterial Competition in Milk. Frontiers in Microbiology, 9. doi:10.3389/fmicb.2018.01148
dc.identifier.issn1664-302X
dc.identifier.pmid29915567
dc.identifier.doi10.3389/fmicb.2018.01148
dc.identifier.urihttp://hdl.handle.net/10754/671100
dc.description.abstractMilk and dairy products harbor a wide variety of bacterial species that compete for both limited resources and space. Under these competitive conditions, bacteria develop specialized mechanisms to protect themselves during niche colonization and nutrient acquisition processes. The bacterial antagonism mechanisms include the production of antimicrobial agents or molecules that facilitate competitor dispersal. In the present work, a bacterial strain designated RC6 was isolated from Ricotta and identified as $\textit{Bacillus cereus}$. It generates antimicrobial peptide (AMP) when grown in the presence of casein. The AMP was active against several species of $\textit{Bacillus}$ and $\textit{Listeria monocytogenes}$. MALDI-TOF analysis of the RP-HPLC purified fractions and amino acid sequencing revealed a molecular mass of 751 Da comprised of a 6-residue sequence, YPVEPF. BLAST analysis showed that the AMP corresponds to the fractions 114-119 of bovine β-casein and represents the product of a specific proteolysis. Analysis of the purified proteolytic fractions from the $\textit{B. cereus}$ RC6 culture supernatant indicated that the presence of at least two different endoproteases is crucial for the generation of the AMP. Indeed, we were able to identify two new candidate endoproteases by means of genome sequencing and functional assignment using a 3D structural model and molecular docking of misannotated hypothetical proteins. In this light, the capacity of $\textit{B. cereus}$ RC6 to generate antimicrobial peptides from casein, through the production of extracellular enzymes, presents a new model of antagonistic competition leading to niche colonization. Hence, as a dairy product contaminant, this strategy may enable proteolytic $\textit{B. cereus}$ RC6 niche specialization in milk matrices.
dc.description.sponsorshipThis work was supported by a grant from the Tunisian Ministry of Higher Education and Scientific Research within the scope of the laboratory project LR11ES31. The authors extend their sincere gratitude to Danielle Slomberg, Jason Morris and Rachid Hassini for helpful corrections and comments. Professor Daniele Daffonchio (KAUST, SA), is acknowledged for the very supportive conversations and discussions.
dc.publisherFrontiers Media SA
dc.relation.urlhttps://www.frontiersin.org/article/10.3389/fmicb.2018.01148/full
dc.rightsArchived with thanks to Frontiers in microbiology
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectMolecular docking
dc.subjectGenome sequencing
dc.subjectAntimicrobial peptide
dc.subjectB. Cereus
dc.subjectΒ-casein
dc.subject3D Structure Prediction
dc.subjectEndoproteases
dc.titleTwo New Secreted Proteases Generate a Casein-Derived Antimicrobial Peptide in $\textit{Bacillus cereus}$ Food Born Isolate Leading to Bacterial Competition in Milk.
dc.typeArticle
dc.identifier.journalFrontiers in microbiology
dc.identifier.pmcidPMC5994558
dc.eprint.versionPublisher's Version/PDF
dc.contributor.institutionUniversité de la Manouba, ISBST, BVBGR-LR11ES31, Biotechpole Sidi Thabet, Ariana, Tunisia
dc.contributor.institutionAix Marseille University, Centre National de la Recherche Scientifique, ICR UMR 7273, Marseille, France
dc.contributor.institutionAix-Marseille University, CEA, Centre National de la Recherche Scientifique, LEMiRE, UMR 7265, BIAM, Saint-Paul-lez-Durance, France
dc.contributor.institutionAix Marseille Univ, Centre National de la Recherche Scientifique, IMM, Plate-Forme Protéomique, MaP IBiSA Labelled, Marseille, France
dc.contributor.institutionUniversité Tunis El Manar, FST, LMBA (LR03ES03), Campus Universitaire, Tunis, Tunisia
dc.contributor.institutionAix-Marseille University, Centre National de la Recherche Scientifique, Centrale Marseille, iSm2, Marseille, France
dc.identifier.volume9
dc.identifier.issueJUN
dc.identifier.eid2-s2.0-85048046755


This item appears in the following Collection(s)

Show simple item record

Archived with thanks to Frontiers in microbiology
Except where otherwise noted, this item's license is described as Archived with thanks to Frontiers in microbiology