Tomato yellow leaf curl virus (TYLCV) capsid protein (CP) forms the capsule that encapsidates the viral genomic ssDNA. We have analyzed the homotypic interaction capacity of full-length and mutated CP. We found that full-length CP interacts with itself. Truncation of the protein from the C-terminal led to diminution of the self-interaction process. Also, the N-terminal region of the CP seemed to be necessary for the interaction. As the two deletion mutants interacted successfully with the wildtype protein, while they failed to self-interact, we suggest that the N-terminal amino acids interact with amino acids of the C-terminal region. Changes in CP homotypic interaction capacity were detected when mutations in the middle portion of the protein were introduced.
Archives of Virology – Springer Journals
Published: Sep 1, 2001
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