Piscine reovirus encodes a cytotoxic, non-fusogenic, integral membrane protein and previously unrecognized virion outer-capsid proteins.
Piscine reovirus (PRV) is a tentative new member of the family Reoviridae and has been linked to heart and skeletal muscle inflammation in farmed Atlantic salmon (Salmo salar L.). Recent sequence-based evidence suggests that PRV is about equally related to members of the genera Orthoreovirus and Aquareovirus. Sequence similarities have also suggested that PRV might encode a fusion-associated small transmembrane (FAST) protein, which in turn suggests that PRV might be the prototype of a new genus with syncytium-inducing potential. In previous support of this designation has been the absence of identifiable PRV-encoded homologues of either the virion outer-clamp protein of ortho- and aquareoviruses or the virion outer-fibre protein of most orthoreoviruses. In the current report, we have provided experimental evidence that the putative p13 FAST protein of PRV lacks the defining feature of the FAST protein family - the ability to induce syncytium formation. Instead, p13 is the first example of a cytosolic, integral membrane protein encoded by ortho- or aquareoviruses, and induces cytotoxicity in the absence of cell-cell fusion. Sequence analysis also identified signature motifs of the outer-clamp and outer-fibre proteins of other reoviruses in two of the predicted PRV gene products. Based on these findings, we conclude that PRV does not encode a FAST protein and is therefore unlikely to be a new fusogenic reovirus. The presence of a novel integral membrane protein and two previously unrecognized, essential outer-capsid proteins has important implications for the biology, evolution and taxonomic classification of this virus.
Department of Microbiology and Immunology, Dalhousie University, Halifax, NS B3H4R2, Canada.
Tim
T
Key
Department of Microbiology and Immunology, Dalhousie University, Halifax, NS B3H4R2, Canada.
Jolene
J
Read
Department of Microbiology and Immunobiology, Harvard Medical School, Boston, MA 02115, USA.
Max L
ML
Nibert
Department of Pediatrics, Dalhousie University, Halifax, NS B3H4R2, Canada.|Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, NS B3H4R2, Canada.|Department of Microbiology and Immunology, Dalhousie University, Halifax, NS B3H4R2, Canada.
Roy
R
Duncan
D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D036022:Capsid Proteins / Q000235:genetics* / Q000378:metabolism; D045744:Cell Line, Tumor; D049109:Cell Proliferation; D003593:Cytoplasm; D005393:Fish Diseases / Q000821:virology*; D015726:Giant Cells; D008565:Membrane Proteins / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D018165:Orthoreovirus / Q000145:classification / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D010802:Phylogeny; D011993:Recombinant Fusion Proteins; D012087:Reoviridae / Q000737:chemistry / Q000145:classification* / Q000235:genetics / Q000302:isolation & purification; D012088:Reoviridae Infections / Q000662:veterinary* / Q000821:virology; D012474:Salmon; D016415:Sequence Alignment; D014709:Vero Cells; D014771:Virion
D036022:Capsid Proteins; D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins