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Positive correlation between serum immuno-reactivity to Demodex-associated Bacillus proteins and Erythematotelangiectic Rosacea.

Br J Dermatol. 2012 Jun 18;

Authors: O'Reilly N, Menezes N, Kavanagh K

Abstract
Background:  Rosacea is a chronic inflammatory condition that affects the skin of the face and the eyes. Erythematotelangiectic rosacea is characterized by flushing, edema and telangiectasia. Rosacea patients demonstrate elevated densities of Demodex mites in their skin compared to controls. A bacterium (Bacillus oleronius) isolated from a Demodex mites from a patient with papulopustular rosacea has been demonstrated to produce antigenic proteins that may play a role in papulopustular and ocular rosacea. Objectives:  The aim of the work presented here was to establish whether there was a correlation between the reactivity of sera from patients with erythematotelangiectic rosacea to Bacillus antigens and to characterise the proteins to which these patients showed reactivity. Methods:  Serum from patients with erythematotelangiectic rosacea and controls was examined for reactivity to Bacillus proteins by Western blot analysis. Proteins to which the sera reacted were excised from gels, trypsin digested and putative identities were assigned following LC/MS analysis. Results:  Eighty per cent (80%, 21/26) of patients with erythematotelangiectic rosacea showed sera reactivity to the 62 and 83kDa proteins of B.oleronius compared to 40% (9/22) of controls (p = 0.004). The 62kDa protein was characterized by LC mass spectrometry to show homology to groEL chaperonin which provokes a strong immune response in mammals. The 83kDa protein showed homology to aconitate hydratase which is increased in expression in bacteria under oxidative stress and is highly immunogenic. Conclusions:  The majority of patients with erythematotelangiectic rosacea show sera reactivity to two proteins from B.oleronius so suggesting that this bacterium may play a role in the induction of this condition. The two proteins to which patient sera reacted were found to be similar to a heat shock protein and an enzyme involved in regulating the stress response of the bacterium.

PMID: 22709541 [PubMed - as supplied by publisher]

http://www.ncbi.nlm.nih.gov/PubMed/22709541?dopt=Abstract = URL to article

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