Dự đoán in silico các epitope tế bào B có tính kháng nguyên trên protein FepA của vi khuẩn Acinetobacter baumannii

Acinetobacter baumannii (A. baumannii) represents a formidable challenge in global health due to its increasing prevalence as a nosocomial pathogen and its notorious multidrug resistance. The absence of a commercially available vaccine underscores the urgent need for effective preventive strategies. Identifying suitable antigenic targets is paramount for vaccine development. This study leverages advanced in silico approaches to systematically predict and characterize potential B-cell epitopes on the FepA protein of A. baumannii, a key outer membrane protein, thereby providing crucial insights for rational vaccine design. This work contributes to addressing the critical public health threat posed by this bacterium.

Các nhà nghiên cứu vi sinh, miễn dịch học, vắc-xin học, tin sinh học và các chuyên gia y tế công cộng.

This study addresses the urgent need for new strategies to combat Acinetobacter baumannii (A. baumannii), a critical nosocomial pathogen with extensive antibiotic resistance, by focusing on vaccine development. Utilizing a comprehensive in silico prediction methodology, researchers investigated the FepA protein, an outer membrane protein of A. baumannii, to identify potential B-cell epitopes. The methodology involved detailed analyses of FepA's antigenicity, solubility, transmembrane topology, and the prediction of both linear and conformational B-cell epitopes using various bioinformatics tools. Subsequently, the identified epitopes were rigorously evaluated for allergenicity, toxicity, physicochemical properties, and homology to human proteins to ensure their suitability for vaccine applications. The findings reveal that FepA is a highly antigenic outer membrane protein containing 22 transmembrane β-barrels. Six optimal epitopes were identified, comprising two linear (E3, E9) and four conformational (E12-E15) epitopes, all demonstrating high immunogenic potential. Crucially, these epitopes were predicted to be non-allergenic and non-toxic (with minor exceptions for E11 in AllerTOP analysis), exhibited favorable physicochemical properties, and showed high conservation (≥90%) across 239 A. baumannii strains. Furthermore, BLASTp analysis confirmed the absence of significant homology to human proteins, minimizing potential autoimmune reactions. This research confirms FepA as an epitope-rich antigen, strongly positioning it as a promising candidate for the development of an effective vaccine against A. baumannii. The results lay a scientific foundation for future experimental validation and vaccine design efforts, offering a pathway to mitigate the burden of infections caused by this challenging pathogen.