The African swine fever virus (ASFV) encodes numerous proteins characterized by complex immune escape mechanisms. At present, the structure and function of these proteins, including the F317L protein, have yet to be fully elucidated. In this study, we examined the immunogenicity of the F317L protein. Mice were subcutaneously immunized with the F317L protein using initial and subsequent booster doses, and, at the 28th day post-treatment, we assessed the humoral and cellular immune responses of mice. The F317L protein stimulated production of specific antibodies and activated humoral immune responses. In addition, F317L stimulated the production of large amounts of IFN-γ by splenic lymphocytes, thereby activating cellular immune responses. Using informatics technology, we predicted and synthesized 29 F317L protein T cell epitopes, which were screened using IFN-γ ELISpot. Among these, the F25 (SRRSLVNPWT) peptide was identified as having a stronger stimulatory effect than the full-length protein. Collectively, our findings revealed that the ASFV F317L protein can stimulate both strong humoral and cellular immunity in mice, and that the F25 (SRRSLVNPWT) peptide may be a potential active T cell epitope. These findings will provide a reference for further in-depth studies of the F317L protein and screening of antigenic epitopes.
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http://dx.doi.org/10.3390/ani14091331 | DOI Listing |
Vaccines (Basel)
December 2024
State Key Laboratory for Animal Disease Control and Prevention, National African Swine Fever Para-Reference Laboratory, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin 150069, China.
Background/objectives: African swine fever (ASF), caused by African swine fever virus (ASFV), poses a significant threat to the global swine industry. This underscores the urgent need for safe and effective ASF vaccines.
Methods: Here, we constructed five bacterium-like particles (BLPs) that each display one of the five ASFV antigens (F317L, H171R, D117L, B602L, and p54) based on the Gram-positive enhancer matrix-protein anchor (GEM-PA) system.
Malays J Pathol
December 2024
National Institutes of Health, Institute for Medical Research, Cancer Research Centre, Haematology Unit, 40170 Shah Alam, Selangor, Malaysia.
Introduction: The emergence of mutations in the BCR::ABL1 kinase domain (KD) impairs imatinib mesylate (IM) binding capacity, thus contributing to IM resistance. Identification of these mutations is important for treatment decisions and precision medicine in chronic myeloid leukaemia (CML) patients. Our study aims to determine the frequency of BCR::ABL1 KD mutations in CML patients with IM resistance.
View Article and Find Full Text PDFLeukemia
November 2024
Centre for Haematology, Faculty of Medicine, Imperial College London, London, United Kingdom.
Vet Microbiol
November 2024
State Key Laboratory for Animal Disease Control and Prevention Harbin Veterinary Research Institute, CAAS, 678 Haping Road, Harbin, Heilongjiang 150069, China. Electronic address:
African swine fever (ASF), a highly infectious and devastating disease affecting both domestic pigs and wild boars, owes its etiology to African swine fever virus (ASFV). ASFV encodes more than 165 proteins. However, novel immunogenic proteins remain unknown.
View Article and Find Full Text PDFAnimals (Basel)
April 2024
Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
The African swine fever virus (ASFV) encodes numerous proteins characterized by complex immune escape mechanisms. At present, the structure and function of these proteins, including the F317L protein, have yet to be fully elucidated. In this study, we examined the immunogenicity of the F317L protein.
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