LL-37: A Drug Target and Biomarker (G820)

Target Name: CAMP

NCBI ID: G820

LL-37: A Drug Target and Biomarker

LL-37, also known as hCAP18, or CAMP, is an antimicrobial peptide (AMP) that plays a crucial role in protecting the skin against S. aureus infection. LL-37 works in various ways to defend against S. aureus:

Direct inhibition and killing of S. aureus: LL-37 can directly inhibit and kill S. aureus bacteria.

Cooperation with other AMPs: LL-37 can cooperate with host-derived AMPs like hCAP18/LL-37 and dermcidin-derived peptides DCD-1(L) to effectively kill S. aureus.

Induction of innate immune response: LL-37 prompts an innate immune response in the skin, leading to the recruitment of phagocytic immune cells that help eliminate potential invading pathogens.

Amplification of innate immune response: The innate immune response triggered by LL-37 can be greatly enhanced by factors derived from the skin commensal S. epidermidis.

Furthermore, the study reveals that lugdunin, a compound with both immunomodulatory and bactericidal activities, offers multi-level protection against S. aureus. Additionally, it is noteworthy that Bacillus subtilis, along with S. aureus, is susceptible to lugdunin and lugdunin/DCD-1(L) combinations. The presence of other microbiota- or host-derived factors can amplify the protective effects of lugdunin.

In summary, LL-37 (or hCAP18) plays a critical role in safeguarding the skin against S. aureus infection through multiple mechanisms. Lugdunin, in combination with LL-37 and other factors, provides robust protection against S. aureus and potentially other bacteria.

Protein Name: Cathelicidin Antimicrobial Peptide

Functions: Antimicrobial protein that is an integral component of the innate immune system (PubMed:22879591, PubMed:16637646, PubMed:18818205, PubMed:9736536, PubMed:14978112). Binds to bacterial lipopolysaccharides (LPS) (PubMed:16637646, PubMed:18818205). Acts via neutrophil N-formyl peptide receptors to enhance the release of CXCL2 (PubMed:22879591). Postsecretory processing generates multiple cathelicidin antimicrobial peptides with various lengths which act as a topical antimicrobial defense in sweat on skin (PubMed:14978112). The unprocessed precursor form, cathelicidin antimicrobial peptide, inhibits the growth of Gram-negative E.coli and E.aerogenes with efficiencies comparable to that of the mature peptide LL-37 (in vitro) (PubMed:9736536)

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