NMR structure determination picornavirus proteins
||NMR structure determination picornavirus proteins|
||SNIC Small Compute|
||Alexandra Ahlner <email@example.com>|
||2022-09-19 – 2023-10-01|
Picornaviruses is a large and diverse family of non-enveloped RNA viruses which are the cause of several human and animal diseases such as polio, common cold and foot-and-mouth disease. After infection the genome is translated into a single polypeptide chain that is further processed and cleaved into structural proteins building the viral capsid and non-structural proteins with different function to fulfil the viral lifecycle. One group of non-structural proteins is the 2A’s which show a considerable divergence both in sequence and in function among the picornaviruses. Some of them, contains a conserved Hbox/NC motif and appears to be related to a group of human Phospholipases, PLAAT1-5. Recently, PLAAT3 was identified as an essential host factor for certain picornavirus containing other types of the 2A-protein. PLAAT3 enables genome transfer into the cytoplasm of the host cell early in the infection cycle. Picornaviruses containing with a 2AHbox/NC-protein can though infect cells independently of PLAAT3.
By investigating the structure of 2AHbox/NC proteins we aim to understand their role in the viral lifecycle and to find the structural mechanism allowing them to by-pass PLAAT3 as a host factor. Here we aim to use PReSTO software to assign the NMR indata, perform a structure calculation and the refine the calculated structure of TuAsV 2A3 to track both structured and flexible parts of the protein.