Bioscience Evidence 2024, Vol.14, No.5, 227-237 http://bioscipublisher.com/index.php/be 229 fusion and endosomal exit of virions (García-Dorival et al., 2023). Additionally, proteomic technology has been employed to examine ASFV-infected cells, identifying infection-associated proteins and their potential roles in pathogenesis (Alfonso et al., 2004). Figure 1 Schematic overview of cellular pathways modulated by ASFV (Adopted from Dolata et al., 2023) Image caption: The pathways have been reproduced and simplified from KEGG pathway maps for endocytosis (hsa04144), cytosolic DNA-sensing (cGAS-STING) pathway (hsa04623), JAK-STAT signaling pathway (hsa04630), and NF-ĸB (hsa04064) and NFAT (hsa04660) signaling pathways. Viral proteins are marked in red font, and host proteins are in blue boxes. The effects caused by the interactions between proteins are represented by the edges and explained in the legend. Created with BioRender.com. * CD163 and SIGLEC1 are considered to act together as potential receptors for ASFV entry (Adopted from Dolata et al., 2023) 3.2 Techniques used in proteomic studies Proteomic studies of ASFV have utilized various advanced techniques to analyze the viral proteome. Key methods include: Mass Spectrometry (MS): This technique is widely used for the identification and quantification of proteins. It has been employed to study the interactome of ASFV proteins and to identify cellular proteins modified in response to ASFV infection (Alfonso et al., 2004; García-Dorival et al., 2023). Affinity Purification: This method is used in conjunction with MS to isolate and identify protein-protein interactions, providing insights into the molecular pathways involved in ASFV infection (García-Dorival et al., 2023).
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