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The F13 residue is critical for interaction among the coat protein subunits of papaya mosaic virus
Author(s) -
Laliberté Gagné M. E.,
Lecours K.,
Gagné S.,
Leclerc D.
Publication year - 2008
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2008.06306.x
Subject(s) - residue (chemistry) , monomer , coat protein , amino acid , escherichia coli , rna , chemistry , biology , biochemistry , gene , organic chemistry , polymer
Papaya mosaic virus (PapMV) coat protein (CP) in Escherichia coli was previously showed to self‐assemble in nucleocapsid‐like particles (NLPs) that were similar in shape and appearance to the native virus. We have also shown that a truncated CP missing the N‐terminal 26 amino acids is monomeric and loses its ability to bind RNA. It is likely that the N‐terminus of the CP is important for the interaction between the subunits in self‐assembly into NLPs. In this work, through deletion and mutation analysis, we have shown that the deletion of 13 amino acids is sufficient to generate the monomeric form of the CP. Furthermore, we have shown that residue F13 is critical for self‐assembly of the CP subunits into NLPs. The replacement of F13 with hydrophobic residues (L or Y) generated mutated forms of the CP that were able to self‐assemble into NLPs. However, the replacement of F13 by A, G, R, E or S was detrimental to the self‐assembly of the protein into NLPs. We concluded that a hydrophobic interaction at the N‐terminus is important to ensure self‐assembly of the protein into NLPs. We also discuss the importance of F13 for assembly of other members of the potexvirus family.