Decapod　iridescent　virus　1　(DIV1)　is　one　of　the　major　pathogens　of　farmed　shrimp.　In　this　study,　the　structural　proteins　of　DIV1　were　analyzed　by　mass　spectrometry.　DIV1　virions　were　purified　from　the　hemolymph　of　artificially　infected　Cherax　quadricarinatus.　The　viral　proteins　were　separated　by　sodium　dodecyl　sulfatepolyacrylamide　gel　electrophoresis,　and　a　total　of　28　protein　bands　were　obtained.　These　protein　bands　were　in-gel　digested　with　trypsin　and　the　resulting　tryptic　peptide　mixtures　were　subjected　to　liquid　chromatography　with　tandem　mass　spectrometry　analysis.　Thirty　virus-encoded　proteins　were　identified.　Among　them,　6　proteins　were　predicted　to　contain　transmembrane　domains,　3　proteins　were　predicted　to　contain　an　Arg-Gly-Asp　motif.　Nine　proteins　showed　significant　homology　with　functionally　characterized　proteins.　Antibodies　were　produced　for　these　candidate　proteins　and　23　of　them　were　confirmed　to　be　the　components　of　DIV1　virions　by　Western　blotting.　This　study　provides　the　first　proteomic　analysis　of　DIV1,　which　establishes　a　foundation　for　further　investigation　of　viral　infection　and　replication.