Interaction of Nipah virus matrix protein with cellular AP3B1
Open Access
- Author:
- Khaw, Wei Young
- Area of Honors:
- Biotechnology
- Degree:
- Bachelor of Science
- Document Type:
- Thesis
- Thesis Supervisors:
- Anthony Paul Schmitt, Thesis Supervisor
Richard John Frisque, Thesis Supervisor
David Scott Gilmour, Thesis Honors Advisor
Dr. Wendy Hanna-Rose, Faculty Reader - Keywords:
- Paramyxovirus
Nipah virus
matrix protein
AP3B1
virus-like particle
virus budding - Abstract:
- Paramyxovirus matrix (M) protein contributes to viral particle assembly and budding through its ability to interact with viral glycoproteins and ribonucleoprotein (RNP) complexes. For efficient budding to take place, M protein could also be a key player in recruiting host cell factors. Affinity co-purification screening has identified the beta subunit of adaptor protein AP3 complex (AP3B1) as a cellular binding partner of Henipavirus M proteins. Furthermore, short M-binding, AP3B1-derived polypeptides were shown to inhibit M protein function and prevent the release of virus-like particles (VLPs) from transfected cells. Here, we performed a series of biochemical experiments to study the interaction between AP3B1 and Nipah virus (NiV) M protein. We found that M-binding, AP3B1-derived polypeptides impair NiV M protein association with cellular membranes, thereby providing mechanistic insight into the inhibition of VLP production observed earlier. In addition, the binding interface within NiV M protein was mapped to amino acid (aa) residues 191-282, as assessed by a series of co-immunoprecipitation binding experiments. Finally, several mutated versions of M-binding, AP3B1-derived polypeptides were constructed, and these would facilitate further mapping studies in the future.