Abstract. Delayed graft function (DGF) is the need for dialysis in the first week after transplantation. Studied were risk factors for DGF in adult (age Ն16 yr) cadaveric renal transplant recipients by means of a multivariable modeling procedure. Only donor and recipient factors known before transplantation were chosen so that the probabilities of DGF could be calculated before transplantation and appropriate preventative measures taken. Data on 19,706 recipients of cadaveric allografts were obtained from the United States Renal Data System registry (1995 to 1998). Graft losses within the first 24 h after surgery were excluded from the analysis (n ϭ 89). Patients whose DGF information was missing or unknown (n ϭ 2820) and patients missing one or more candidate predictors (n ϭ 2951) were also excluded. By means of a multivariable logistic regression analysis, factors contributing to DGF in the remaining 13,846 patients were identified. After validating the logistic regression model, a nomogram was developed as a tool for identifying patients at risk for DGF. The incidence of DGF was 23.7%. Sixteen independent donor or recipient risk factors were found to predict DGF. A nomogram quantifying the relative contribution of each risk factor was created. This index can be used to calculate the risk of DGF for an individual by adding the points associated with each risk factor. The nomogram provides a useful tool for developing a pretransplantation index of the likelihood of DGF occurrence. With this index in hand, better informed treatment and allocation decisions can be made.
This study examines the contribution of the fusion (F) and hemagglutinin-neuraminidase (HN) glycoprotein genes of bovine parainfluenza virus type 3 (BPIV3) to its restricted replication in the respiratory tract of nonhuman primates. A chimeric recombinant human parainfluenza type 3 virus (HPIV3) containing BPIV3 F and HN glycoprotein genes in place of its own and the reciprocal recombinant consisting of BPIV3 bearing the HPIV3 F and HN genes (rBPIV3-F H HN H ) were generated to assess the effect of glycoprotein substitution on replication of HPIV3 and BPIV3 in the upper and lower respiratory tract of rhesus monkeys. The chimeric viruses were readily recovered and replicated in simian LLC-MK2 cells to a level comparable to that of their parental viruses, suggesting that the heterologous glycoproteins were compatible with the PIV3 internal proteins. HPIV3 bearing the BPIV3 F and HN genes was restricted in replication in rhesus monkeys to a level similar to that of its BPIV3 parent virus, indicating that the glycoprotein genes of BPIV3 are major determinants of its host range restriction of replication in rhesus monkeys. rBPIV3-F H HN H replicated in rhesus monkeys to a level intermediate between that of HPIV3 and BPIV3. This observation indicates that the F and HN genes make a significant contribution to the overall attenuation of BPIV3 for rhesus monkeys. Furthermore, it shows that BPIV3 sequences outside the F and HN region also contribute to the attenuation phenotype in primates, a finding consistent with the previous demonstration that the nucleoprotein coding sequence of BPIV3 is a determinant of its attenuation for primates. Despite its restricted replication in the respiratory tract of rhesus monkeys, rBPIV3-F H HN H conferred a level of protection against challenge with HPIV3 that was indistinguishable from that induced by previous infection with wild-type HPIV3. The usefulness of rBPIV3-F H HN H as a vaccine candidate against HPIV3 and as a vector for other viral antigens is discussed.Bovine parainfluenza virus type 3 (BPIV3) is restricted in replication in the respiratory tract of rhesus monkeys, chimpanzees, and humans, and it is being evaluated as a vaccine against human PIV3 (HPIV3) (8,10,12,26,27). HPIV3 and BPIV3 are closely related enveloped, nonsegmented, negativestrand RNA viruses within the Respirovirus genus of the Paramyxoviridae family (2, 10). The two viruses are 25% related antigenically by cross-neutralization studies (8), and they share neutralization epitopes on their fusion (F) and hemagglutininneuraminidase (HN) surface glycoproteins (9, 30). HPIV3 and BPIV3 are essentially identical in genome organization (2). Both viruses encode nine proteins: the nucleoprotein (N), phosphoprotein (P), and large polymerase protein (L) are nucleocapsid-associated proteins; the C, D, and V accessory proteins are proteins of unknown function encoded by the P mRNA or by an edited version thereof; the M protein is an internal matrix protein; and the F and HN glycoproteins are protective antigens of the vi...
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