Asset Details
Do you wish to reserve the book?
An antimicrobial daptide from human skin commensal Staphylococcus hominis protects against skin pathogens
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
An antimicrobial daptide from human skin commensal Staphylococcus hominis protects against skin pathogens
Do you wish to request the book?
An antimicrobial daptide from human skin commensal Staphylococcus hominis protects against skin pathogens
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
An antimicrobial daptide from human skin commensal Staphylococcus hominis protects against skin pathogens
2025
Overview
Coagulase-negative staphylococci are dominant human skin colonizers, producing natural products that shape the community and prevent pathogen colonization. The molecular mechanisms by which these natural products mediate interbacterial competition are not fully understood. Here, we identify a plasmid-borne daptide bacteriocin (hominicin) from a human skin isolate of
Staphylococcus hominis
, which features an unusual
N
2
-
N
2
-dimethyl-1,2-propanediamine C-terminus. Heterologous expression of the reconstituted biosynthetic loci yields a daptide product of the same molecular mass that exhibits antimicrobial activity against the skin pathogen
Staphylococcus aureus
, with amino-modified termini being essential for activity. Membrane permeability and voltage-clamp lipid bilayer experiments support a mechanism by which the daptide rapidly dissipates the transmembrane potential by forming peptidic channels. Additionally, we identify a cognate
homI
gene that confers resistance against membrane damage. Finally, the purified daptide effectively protects mouse skin from
S. aureus-
induced epicutaneous injury, as evidenced by reduced bacterial burden, inflammation, and transepithelial water loss, highlighting its therapeutic potential for treating bacterial skin infections. Our findings elucidate a mechanism of action, biosynthesis, and resistance for a staphylococcal bacteriocin belonging to a class of natural products called daptides.
Coagulase-negative staphylococci secrete natural products that prevent pathogen colonization. Here, the authors identify hominicin, a daptide bacteriocin produced by
Staphylococcus hominis
that has antimicrobial activity against a skin pathogen.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 140/58
/ 38
/ 38/39
/ 38/44
/ 45
/ 64/60
/ 82/83
/ 9/97
/ Animals
/ Anti-Bacterial Agents - pharmacology
/ Bacteria
/ Enzymes
/ Female
/ Genomes
/ Humanities and Social Sciences
/ Humans
/ Lipids
/ Mice
/ NMR
/ Peptides
/ Plasmids
/ Science
/ Skin
/ Staphylococcal Skin Infections - drug therapy
/ Staphylococcal Skin Infections - microbiology
/ Staphylococcus aureus - drug effects
/ Staphylococcus hominis - genetics
/ Staphylococcus hominis - isolation & purification
