Genocide and the International Court of Justice: Finally, a Duty to Prevent the Crime of Crimes

The International Court of Justice has issued its long-awaited decision in the suit filed by Bosnia and Herzegovina against Serbia and Montenegro with respect to the 1992–1995 war. The decision confirms the factual and legal determinations of the International Criminal Tribunal for the former Yugoslavia, ruling that genocide was committed during the Srebrenica massacre in July 1995 but that the conflict as a whole was not genocidal in nature. The Court held that Serbia had failed in its duty to prevent genocide in Srebrenica, although—because, the Court said, there was no certainty that it could have succeeded in preventing the genocide—no damages were awarded. The judgment provides a strong and authoritative statement of the general duty upon states to prevent genocide that dovetails well with the doctrine of the responsibility to protect.

Mentally disordered offenders and the European Court of Human Rights

This article presents the findings from a study of cases taken to the European Court of Human Rights by mentally disordered offenders. The issues raised include the problems raised by indeterminate sentences, the use of detention for preventive purposes, and debates about treatment. The countries represented are Belgium, Norway, Poland, the Netherlands, Russia and the United Kingdom.

ADP-Ribose-1"-Monophosphatase: a Conserved Coronavirus Enzyme That Is Dispensable for Viral Replication in Tissue Culture

Replication of the ~30-kb plus-strand RNA genome of coronaviruses and synthesis of an extensive set of subgenome-length RNAs are mediated by the replicase-transcriptase, a membrane-bound protein complex containing several cellular proteins and up to 16 viral nonstructural proteins (nsps) with multiple enzymatic activities, including protease, polymerase, helicase, methyltransferase, and RNase activities. To get further insight into the replicase gene-encoded functions, we characterized the coronavirus X domain, which is part of nsp3 and has been predicted to be an ADP-ribose-1"-monophosphate (Appr-1"-p) processing enzyme. Bacterially expressed forms of human coronavirus 229E (HCoV-229E) and severe acute respiratory syndrome-coronavirus X domains were shown to dephosphorylate Appr-1"-p, a side product of cellular tRNA splicing, to ADP-ribose in a highly specific manner. The enzyme had no detectable activity on several other nucleoside phosphates. Guided by the crystal structure of AF1521, an X domain homolog from Archaeoglobus fulgidus, potential active-site residues of the HCoV-229E X domain were targeted by site-directed mutagenesis. The data suggest that the HCoV-229E replicase polyprotein residues, Asn 1302, Asn 1305, His 1310, Gly 1312, and Gly 1313, are part of the enzyme's active site. Characterization of an Appr-1"-pase-deficient HCoV-229E mutant revealed no significant effects on viral RNA synthesis and virus titer, and no reversion to the wild-type sequence was observed when the mutant virus was passaged in cell culture. The apparent dispensability of the conserved X domain activity in vitro indicates that coronavirus replicase polyproteins have evolved to include nonessential functions. The biological significance of the novel enzymatic activity in vivo remains to be investigated.