Comparison of the primary sequence of spring viremia of carp virus M protein with that of vesicular stomatitis virus.

The nucleotide sequence of Spring viremia of carp virus mRNA coding for the matrix protein (M) has been determined from a complete DNA copy cloned in the Escherichia coli plasmid pBR322. The clone is 710 nucleotides long and, excluding the 3' homopolymeric end (representing the mRNA polyadenylic acid sequence), encodes a protein of some 223 amino acids (25,600 Da). The protein has more basic than acidic amino acids and no significant amino- or carboxy-terminal hydrophobic domains. The predicted amino acid sequence of the M protein of Spring viremia of carp virus can be aligned with that of vesicular stomatitis virus, revealing a significant amount of homology (28%). The carboxy-terminal regions of the two proteins exhibit much less homology than their amino termini.