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Volume 11, Number 1—January 2005
Dispatch

A Novel Paramyxovirus?

Christopher F. Basler*Comments to Author , Adolfo García-Sastre*, and Peter Palese*
Author affiliations: *Mount Sinai School of Medicine, New York, New York, USA

Main Article

Figure 1

Angrem52 and Angrem104 appear to be paramyxovirus genes. A) Gene positions of a generic paramyxovirus and predicted genome position of Angrem104 (top), the phosphoprotein (P) gene, Angrem52 (bottom), the matrix protein (M) and fusion protein (F) genes. A potential editing site (nucleotides 783–795), which might allow production from the OPmV P gene of V and W/D proteins, is shown in genomic (negative) sense aligned with the proposed editing sites of Nipah virus (NC_002728) (1) and Hendra viruses

Figure 1. Angrem52 and Angrem104 appear to be paramyxovirus genes. A) Gene positions of a generic paramyxovirus and predicted genome position of Angrem104 (top), the phosphoprotein (P) gene, Angrem52 (bottom), the matrix protein (M) and fusion protein (F) genes. A potential editing site (nucleotides 783–795), which might allow production from the OPmV P gene of V and W/D proteins, is shown in genomic (negative) sense aligned with the proposed editing sites of Nipah virus (NC_002728) (1) and Hendra viruses (NC_001906). The full-length P open reading frame (ORF) was obtained by inserting an additional nucleotide in the reported Angrem104 sequence (see text). Angrem52 is predicted to be a “read-through” product of the M and F genes, a novel paramyxovirus. The full-length F ORF was obtained by making 5 changes to the reported Angrem52 sequence (see text). Putative gene-end, intergenic (IG), and gene-start transcription regulatory signals lying between OPmV M and F genes are shown aligned to the corresponding signals from Nipah and Hendra virus (shown in genomic sense [12]). B) The putative OPmV F protein contains a fusion peptide. The sequences surrounding the F protein cleavage sites, including most fusion peptides, of several paramyxoviruses, including putative OPmV, were aligned by using the AlignX program of the Vector NTI6 software package. The arrow indicates the cleavage site. Residues in red are absolutely conserved. Residues in blue are conserved in most sequences. C) Putative genome organization of the putative OPmV P gene, allowing translation of P, V, W, and C ORFs. D) Alignment of cysteine-rich carboxy-termini of the putative OPmV and Nipah virus V proteins. The conserved carboxy-terminal regions of the V proteins were aligned by using the AlignX program of the Vector NTI6 software package. Conserved residues are indicated in red, except for conserved cysteines, which are in blue. Underlined residues are conserved among all paramyxovirus V proteins.

Main Article

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