Abstract
Acne vulgaris is a disorder affecting the pilosebaceous unit resulting in both inflammatory and non-inflammatory clinical lesions. Cutibacterium acnes (C. acnes) of a specific lineage, plays a key role in inflammatory acne by producing several virulence factors thereby increasing their inflammatory capacity. The C. acnes mutated CAMP1 factor display strong TLR-2 binding property in highly inflammatory C. acnes strains. CAMP1 peptide array analysis of 116 15-mer peptides sequences with an overlap of 11 amino acids, were immobilized onto glass plate and showed that seven peptides (A14, A15, B1, B2, B3, C1 and C3) were specifically recognized by TLR-2 and located on the same side of the in silico 3D-CAMP1 structure.
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