BOR-SHOW TZANGYI-JU LEETSAI-CHING HSU2026-10-162026-10-162009-01-01Pure ID: 15455851Pure UUID: 939afef3-6a95-4e91-9c16-c37b9c87875110.1186/1423-0127-16-13https://www.scopus.com/pages/publications/63449124484https://scholars.csmu.edu.tw/handle/123456789/23408Background. Activity of secreted phospholipase A (sPLA2) has been implicated in a wide range of cellular responses. However, little is known about the function of human parvovirus B19-VP1 unique region (VP1u) with sPLA2 activity on macrophage. Methods. To investigate the roles of B19-VP1u in response to macrophage, phospholipase A2 activity, cell migration assay, phagocytosis activity, metalloproteinase assay, RT-PCR and immunoblotting were performed. Results. In the present study, we report that migration, phagocytosis, IL-6, IL-1 mRNA, and MMP9 activity are significantly increased in RAW264.7 cells by B19-VP1u protein with sPLA2 activity, but not by B19-VP1uD175A protein that is mutated and lacks sPLA2 activity. Additionally, significant increases of phosphorylated ERK1/2 and JNK proteins were detected in macrophages that were treated with B19-VP1u protein, but not when they were treated with B19-VP1uD175A protein. Conclusion. Taken together, our experimental results suggest that B19-VP1u with sPLA2 activity affects production of IL-6, IL-1 mRNA, and MMP9 activity, possibly through the involvement of ERK1/2 and JNK signaling pathways. These findings could provide clues in understanding the role of B19-VP1u and its sPLA2 enzymatic activity in B19 infection and B19-related diseases.enjournal article