Like other paramyxoviruses, the P gene of henipaviruses produces multiple proteins which play a key role in viral evasion of host innate immune responses [4, 40, 41] . One of these is the Cys-rich V protein: all members of the subfamily Paramyxovirinae produce the V protein with the exception of the human parainfluenza virus 1 (hPIV1). Although a putative RNA editing sequence (AAGAGGG) is present at the expected editing site of the P gene, the hPIV1 RNA polymerase does not produce an edited mRNA of the P gene [42] . There are remnants of the V ORF easily detectable in the hPIV1 P gene although the predicted 68-aa ORF region is interrupted by multiple in-frame stop codons. Of the 7 Cys residues conserved between bovine parainfluenza virus 3 and Sendai virus, four are still present in the non-functional V ORF of hPIV1 [42] . In contrast, an extensive ORF and sequence homology search of the CedPV P gene only identified one aa coding region with minimal sequence identity to the V ORFs of HeV and NiV (see Fig. S8 ). In this region, out of the 9 Cys residues conserved between HeV and NiV V proteins, only 2 are present in the CedPV P gene. Furthermore, the sequence (AGATGAG) upstream from this putative ORF V coding region does not match the consensus RNA editing site. It can therefore be concluded that CedPV is the only member of Paramyxovirinae which lacks both the functional V mRNA/protein and the coding capacity for the RNA editing site and ORF V. The evolutionary significance of this finding needs further investigation.