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Utilizing of quantitative proteomics to identify species-specific protein therapeutic target for treatment of leishmaniasis.

ABSTRACT: Identification of common Leishmania antigen proteins is important for practical purposes ranging from diagnostic to the development of a vaccine for the prevention of leishmaniasis. Moreover, we need to establish the potential drug targets that interrupt the replication and transmission of the pathogen to promote drug discovery. Therefore, the objective of this work was to provide the public proteome database which would be useful for the establishment of novel protein antigenicity for therapeutic purposes. This information would introduce the alternative protein targets for Leishmaniasis, allowing the development of therapeutic strategies for the disease.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Leishmania Donovani Ld 2001

TISSUE(S): Cell Culture, Diploid Cell

DISEASE(S): Leishmaniasis

SUBMITTER: Sucheewin Krobthong

LAB HEAD: Kiattawee Choowongkomon

PROVIDER: PXD026304 | Pride | 2022-05-20

REPOSITORIES: Pride

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Publications

Utilizing Quantitative Proteomics to Identify Species-Specific Protein Therapeutic Targets for the Treatment of Leishmaniasis.

Krobthong Sucheewin S Yingchutrakul Yodying Y Samutrtai Pawitrabhorn P Hitakarun Atitaya A Siripattanapipong Suradej S Leelayoova Saovanee S Mungthin Mathirut M Choowongkomon Kiattawee K

ACS omega 20220404 15

Leishmaniasis is a tropical disease caused by Leishmania parasites, which are transmitted through the bites of infected sandflies. We focused on the emergence of leishmaniasis in Thailand caused by a species (Leishmania orientalis). Treatment by chemotherapy is not effective against L. orientalis. Hence, we intended to solve this issue using a proteomics approach to investigate protein profiles and in silico analysis for the identification of antigenic proteins from < ...[more]

PMID: 35474788

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Project description:Herein we demonstrate the efficacy of an unbiased proteomics screening approach for studying protein expression changes in the KC-Tie2 psoriasis mouse model, identifying multiple protein expression changes in the mouse and validating these changes in human psoriasis. KC-Tie2 mouse skin samples (n=3) were compared with littermate controls (n=3) using gel-based fractionation followed by label-free protein expression analysis. 5482 peptides mapping to 1281 proteins were identified and quantitated: 105 proteins exhibited fold-changes ≥2.0 including: stefin A1 (average fold change of 342.4 and an average P = 0.0082; cystatin A, human orthologue); slc25a5 (average fold change of 46.2 and an average P = 0.0318); serpinb3b (average fold change of 35.6 and an average P = 0.0345; serpinB1, human orthologue); and kallikrein related peptidase 6 (average fold change of 4.7 and an average P = 0.2474; KLK6). We independently confirmed mouse gene expression-based increases of selected genes including serpinb3b (17.4-fold, P < 0.0001), KLK6 (9.0-fold, P = 0.002), stefin A1 (7.3-fold; P < 0.001) and slc25A5 (1.5-fold; P = 0.05) using qRT-PCR on a second cohort of animals (n=8). Parallel LC/MS/MS analyses on these same samples verified protein-level increases of 1.3-fold (slc25a5; P < 0.05), 29,000-fold (stefinA1; P < 0.01), 322-fold (KLK6; P < 0.0001) between KC-Tie2 and control mice. To underscore the utility and translatability of our combined approach, we analyzed gene and protein expression levels in psoriasis patient skin and primary keratinocytes vs. healthy controls. Increases in gene expression for slc25a5 (1.8-fold), cystatin A (3.0-fold), KLK6 (5.8-fold) and serpinB1 (76-fold; all P < 0.05) were observed between healthy controls and involved lesional psoriasis skin and primary psoriasis keratinocytes. Moreover slc25a5, cystatin A, KLK6 and serpinB1 protein were all increased in lesional psoriasis skin compared to normal skin. These results highlight the usefulness of preclinical disease models using readily-available mouse skin and demonstrate the utility of proteomic approaches for identifying novel peptides/proteins that are differentially regulated in psoriasis that could serve as sources of auto-antigens or provide novel therapeutic targets for the development of new anti-psoriatic treatments.

Dataset Information

Utilizing of quantitative proteomics to identify species-specific protein therapeutic target for treatment of leishmaniasis.

Publications

Utilizing Quantitative Proteomics to Identify Species-Specific Protein Therapeutic Targets for the Treatment of Leishmaniasis.

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