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The effect of point mutations within the N-terminal domain of Mason-Pfizer monkey virus capsid protein on virus core assembly and infectivity |
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| Authors: | Wildová Marcela Hadravová Romana Stokrová Jitka Krízová Ivana Ruml Tomás Hunter Eric Pichová Iva Rumlová Michaela |
| Affiliation: | a Gilead Sciences and IOCB Research Centre, Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, Flemingovo nám. 2, 166 10, Prague, Czech Republic b Department of Biochemistry and Microbiology and Center of Applied Genomics, Institute of Chemical Technology, Prague, Technická 3, 166 28 Prague, Czech Republic c Yerkes Natural Primate Research Center, Emory Vaccine Center, 954 Gatewood Road, Atlanta GA 30329, USA |
| Abstract: | Retroviral capsid protein (CA) mediates protein interactions driving the assembly of both immature viral particles and the core of the mature virions. Structurally conserved N-terminal domains of several retroviruses refold after proteolytic cleavage into a β-hairpin, stabilized by a salt bridge between conserved N-terminal Pro and Asp residues. Based on comparison with other retroviral CA, we identified Asp50 and Asp57 as putative interacting partners for Pro1 in Mason-Pfizer monkey virus (M-PMV) CA. To investigate the importance of CA Pro1 and its interacting Asp in M-PMV core assembly and infectivity, P1A, P1Y, D50A, T54A and D57A mutations were introduced into M-PMV. The P1A and D57A mutations partially blocked Gag processing and the released viral particles exhibited aberrant cores and were non-infectious. These data indicate that the region spanning residues Asp50-Asp57 plays an important role in stabilization of the β-hairpin and that Asp57 likely forms a salt-bridge with P1 in M-PMV CA. |
| Keywords: | Retrovirus Assembly Capsid protein M-PMV β-hairpin |
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