Kinetoplastid Membrane Protein 11 (KMP-11): A Candidate for Vaccine Development and Serological Detection of Leishmaniasis Introduction Leishmaniasis is a significant public health concern caused by protozoan parasites of the genus Leishmania, transmitted primarily through the bites of infected female sandflies. The disease manifests in various forms, including cutaneous, mucocutaneous, and visceral leishmaniasis, each with distinct clinical features and implications for affected individuals. KMP-11 protein has been highlighted as a potential target for vaccine development or serological detection tool due to its immunogenic properties. This study investigates the physicochemical and antigenic properties of the KMP-11(TPP44494.1) utilizing bioinformatics tools, aiming to evaluate its viability as a candidate for vaccine development and serological detection of Leishmania spp, across diverse host species. Methods The antigenicity, allergenicity, and toxicity of the KMP-11 were assessed using Vaxigen, AllerTop, and ToxinPred servers, respectively. The ProtParam server was employed to analyze the physicochemical characteristics of the protein. Additionally, linear B-cell and cytotoxic T lymphocyte (CTL) epitopes were predicted using the ABCpred webserver and the IEDB database, contributing to a comprehensive understanding of the protein's potential in immunological applications. Results The analysis demonstrated that the KMP-11 is antigenic, with a Vaxigen score of 0.5097, and is classified as non-allergenic and non-toxic. Physicochemical characterization revealed a molecular weight of 25090.30 Daltons and an estimated half-life of 30 hours in mammalian reticulocytes in vitro, over 20 hours in yeast in vivo, and more than 10 hours in Escherichia coli in vivo. Additionally, the aliphatic index of 39.28 suggests that the protein has a moderate level of thermostability, while the theoretical isoelectric point (pI) was determined to be 6.15. The GRAVY index of -1.248 suggests a polar nature with good water interaction, indicating high solubility. The protein comprises 40 negatively charged residues (aspartic acid and glutamic acid) and 35 positively charged residues (arginine and lysine), with a molecular formula of C1112H1686N304O333S14 and a total atom count of 3449. The QuerySol scaled solubility value was determined to be 0.687 indicates that the protein is predicted to have high solubility. Conclusions Our findings identified multiple linear B-cell and cytotoxic T lymphocyte (CTL) epitopes within the KMP-11 protein, all exhibiting high antigenicity, thereby highlighting their potential for application in vaccine development and serological detection of Leishmania spp. Bibliography 1. Kaur, S., & Kaur, H. (2005). Kinetoplastid membrane protein-11 DNA vaccination induces complete protection against visceral leishmaniasis in hamsters. The Journal of Immunology, 174(11), 7160-7167. https://doi.org/10.4049/jimmunol.174.11.7160 2. Zhang, Y., & Liu, Z. (2021). Development of dominant epitope-based vaccines encoding Gp63, Kmp-11 and Amastin with DNA prime-protein boost vaccination strategy against Leishmania infantum. Vaccine, 39(14), 1984-1994. 3. https://doi.org/10.1016/j.vaccine.2021.02.023 Rojas, C., & Valenzuela, J. G. (2024). Advances in Leishmania vaccines: Current development and future directions. Pathogens, 13(9), Article 812. 4. https://doi.org/10.3390/pathogens13090812 Mendez, S., & Ceballos, J. (2015). Kinetoplastid membrane protein-11 as a vaccine candidate and a potential biomarker for leishmaniasis diagnosis. Frontiers in Microbiology, 6, Article 460. https://doi.org/10.3389/fmicb.2015.00460
