Viruslike Particles Encapsidating Respiratory Syncytial Virus M and M2 Proteins Induce Robust T Cell Responses
Benjamin Schwarz, Kaitlyn M Morabito, Tracy J Ruckwardt, Dustin P Patterson, John Avera, Heini M Miettinen, Barney S Graham, Trevor Douglas
ACS Biomaterials Science & Engineering
Subunit vaccines provide a safe, focused alternative to conventional vaccines. However, these vaccines often require significant adjuvants and are particularly hard to target toward cytotoxic T lymphocyte (CTL) immunity. Viruslike particles (VLPs) provide biomaterial scaffolds with pathogen-like polyvalent structures making them useful platforms for biomimetic antigen delivery to the immune system. Encapsidation of antigens within VLPs has been shown to enhance antigen availability for CD8 T cell responses. Here, we examine the potential to generate complex responses to multiple subunit antigens localized within the same VLP particle. Two proteins of respiratory syncytial virus (RSV) with well-characterized CD8 T cell responses, the matrix (M) and matrix 2 (M2) proteins, were successfully coencapsidated within the P22 VLP. Upon intranasal administration in mice, the particles stimulated CD8 T cell memory responses against both antigens. In addition, vaccination elicited tissue-resident T cell populations. Upon subsequent RSV challenge, P22-M/M2-treated mice displayed significantly reduced lung viral titers. This demonstrates the utility of the P22 VLP in directing immune responses to multiple encapsidated viral antigens, demonstrating the potential of this technology to facilitate immunity to multiple targets simultaneously.
How is this information collected?
This collection of Montana State authored publications is collected by the Library to highlight the achievements of Montana State researchers and more fully understand the research output of the University. They use a number of resources to pull together as complete a list as possible and understand that there may be publications that are missed. If you note the omission of a current publication or want to know more about the collection and display of this information email Leila Sterman.