The complement system plays a crucial role in innate defense against invading pathogens. The complement proteolytic cascade on the microbial surface generates potent proinflammatory molecules and opsonins, resulting in lysis of the opsonized microbe or its phagocytosis by innate immune cells. Many pathogens, including viruses, have thus evolved strategies to overcome the complement-mediated destruction, e.g., by hijacking host complement regulators or encoding their own analogues. Since persistent activation of the complement is considered to play a key role in the pathogenesis of in severe coronavirus disease 2019 (COVID-19), we hypothesized that severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) virions subvert normal complement recognition and/or lysis. To test that, we produced SARS-CoV-2 virions in a human cell line naturally permissive to infection and purified them by size exclusion. Analysis of the purified SARS-CoV-2 virions by liquid chromatography coupled to tandem mass spectrometry revealed that SARS-CoV-2 reproducibly incorporates a subset of host cellular proteins, including some of the known complement regulators, into its virions during budding from infected cells. We confirmed the presence of the complement regulators in SARS-CoV-2 virions by Western blotting. Subsequent functional assays using specific blocking antibodies and/or enzymatic cleavage confirmed the role of the hijacked host cellular proteins in prevention of the complement-mediated lysis of SARS-CoV-2 virions. In conclusion, our results reveal an intriguing immune escape mechanism of SARS-CoV-2 with possible implications in the immunopathology of COVID-19