2024/11/04 by Rokaia Sultana, Robert V. Stahelin · 1 citation
Medicine · Mathematics · #SARS-CoV-2 and COVID-19 Research #Long-Term Effects of COVID-19 #COVID-19 epidemiological studies
paper · doi:10.1016/j.virol.2024.110285
Virus-like particles (VLPs) resemble the parent virus but lack the viral genome, providing a safe and efficient platform for the analysis of virus assembly and budding as well as the development of vaccines and drugs. During the COVID-19 pandemic, caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the formation of SARS-CoV-2 VLPs was investigated as an alternative to authentic virions because the latter requires biosafety level 3 (BSL-3) facilities. This allowed researchers to model its assembly and budding processes, examine the role of mutations in variants of concern, and determine how the structural proteins interact with each other. Also, the absence of viral genome in VLPs circumvents worries of gains in infectivity via mutagenesis. This review summarizes the strengths and limitations of several SARS-CoV-2 VLP systems and details some of the strides that have been made in using these systems to study virus assembly and budding, viral entry, and antibody and vaccine development. • SARS-CoV-2 virus-like particles (VLPs) can be handled in BSL-2 facilities circumventing the need for BSL-3 facilities for authentic SARS-CoV-2 studies. • VLPs of SARS-CoV-2 have been produced from different cellular systems to produce VLPs that are used to mechanistically interrogate assembly and budding, virus entry, antibody and immune responses, as well as vaccine development. • There are some differences in reported minimal requirements for SARS-CoV-2 VLP assembly and budding, but most studies indicate that VLPs can be generated consistently and efficiently by the expression of the M, E and N structural proteins. • The SARS-CoV-2 S protein incorporation gives rise to more authentic VLPs that can be tested for interactions with ACE2 and virus entry as well as screening of small molecule and antibody efficacy of inhibiting VLP entry.