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2.
J Virol ; 56(1): 221-6, 1985 Oct.
Article in English | MEDLINE | ID: mdl-4032535

ABSTRACT

The complete nucleotide sequence of RNA segment 7 of influenza C/California/78 virus was determined by using cloned cDNA derived from viral RNA. The gene is 934 nucleotides long and possesses a long open reading frame which can code for a protein of 286 amino acids. Hybrid arrest translation experiments with the cloned cDNA fragment and poly(A)-containing RNA isolated from virus-infected cells showed that a 28,500-molecular-weight protein is coded for by RNA 7. Comparison of the proteins induced in the cell-free system and in virus-infected cells with those found in purified virus suggests that the 28,500-molecular-weight protein is a nonstructural protein.


Subject(s)
Orthomyxoviridae/genetics , RNA, Messenger/genetics , RNA, Viral/genetics , Viral Proteins/genetics , Amino Acid Sequence , Base Sequence , Cell-Free System , Genes, Viral , Molecular Weight , Plasmids , Protein Biosynthesis
3.
Virus Res ; 1(6): 433-41, 1984 Sep.
Article in English | MEDLINE | ID: mdl-6532006

ABSTRACT

The complete nucleotide sequence of RNA segment 5 of the influenza C/California/78 (C/Cal/78) virus was determined by using cloned cDNA derived from viral RNA. The gene contains 1809 nucleotides and can code for a protein of 565 amino acids with a molecular weight of 63 525. The RNA 5 protein of the influenza C/Cal/78 virus possesses two short regions which share a high degree (60-83%) of sequence homology with the nucleoproteins of influenza A and B viruses. These and other structural features of the RNA 5 protein suggest that RNA 5 of influenza C viruses codes for the nucleoprotein. The data also suggest that influenza C viruses are orthomyxoviruses, but that they are more distantly related to either type A or type B viruses than are influenza A and B viruses to each other.


Subject(s)
Nucleoproteins/genetics , Orthomyxoviridae/genetics , RNA, Viral/analysis , Amino Acid Sequence , Base Sequence , Influenza A virus/genetics , Influenza B virus/genetics , Nucleoproteins/analysis
4.
J Virol ; 50(1): 118-24, 1984 Apr.
Article in English | MEDLINE | ID: mdl-6699942

ABSTRACT

The complete nucleotide sequence of the influenza C/California/78 virus RNA 4 was obtained by using cloned cDNA derived from the RNA segment. This gene is 2,071 nucleotides long and can code for a polypeptide of 654 amino acids. Although there are no convincing sequence homologies between RNA 4 and the hemagglutinin genes of influenza A and B viruses, we suggest, on the basis of structural features, that RNA 4 of the influenza C virus codes for the hemagglutinin. The structural features which are common to the hemagglutinins of influenza A, B, and C viruses include (i) a hydrophobic signal peptide, (ii) an arginine cleavage site between the hemagglutinin 1 and 2 subunits, (iii) hydrophobic regions at the amino and carboxyl termini of the hemagglutinin 2 subunit, and (iv) several conserved cysteine residues. Additional evidence that RNA 4 of influenza C virus codes for the hemagglutinin is that the tripeptide Ile-Phe-Gly, known to be present at the amino terminus of the hemagglutinin 2 subunit of influenza C virus, is encoded by RNA 4 at a point immediately adjacent to the presumptive arginine cleavage site. The lack of primary sequence homology between the influenza C virus hemagglutinin and the influenza A or B virus hemagglutinins, which all have similar functions, might be attributed to convergent rather than divergent evolution. However, the structural similarities among the influenza A, B, and C virus hemagglutinins strongly suggest that the three hemagglutinin genes have diverged from a common precursor.


Subject(s)
Genes, Viral , Hemagglutinins, Viral/genetics , Influenza A virus/immunology , Orthomyxoviridae/immunology , RNA, Viral/genetics , Amino Acid Sequence , Base Sequence , Binding Sites , Biological Evolution , Cysteine/analysis , Hemagglutinins, Viral/analysis , Influenza A virus/genetics , Orthomyxoviridae/genetics , Peptides/analysis , Protein Sorting Signals , Sialic Acids/metabolism
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