The psychometric properties of the Italian version of the Hospital Anxiety and Depression Scale and its utility as a screening instrument for anxiety and depression in a non-psychiatric setting were evaluated. The questionnaire was administered twice to 197 breast cancer patients randomised in a phase III adjuvant clinical trial: before the start of chemotherapy and at the first follow-up visit. The presence of psychiatric disorders was evaluated at the follow-up visit using the Structured Clinical Interview for DSM-III-R in 132 patients. Factor analyses identified two strictly correlated factors. Crohnbach's alpha for the anxiety and depression scales ranged between 0.80 and 0.85. At follow-up, 50 patients (38%) were assigned a current DSM-III-R diagnosis, in most cases adjustment disorders (24%) or major depressive disorder (10%). Receiver operating characteristics (ROC) analysis was used to test the discriminant validity for both anxiety and depressive disorders. The comparison of the areas under the curve (AUC) between the two scales did not show any difference in identifying either anxiety (P = 0.855) or depressive disorders (P = 0.357). The 14-item total scale showed a high internal consistency (alpha = 0.89 and 0.88) and a high discriminating power for all the psychiatric disorders (AUC = 0.89; 95% CI = 0.83-0.94). The cut-off point that maximised sensitivity (84%) and specificity (79%) was 10. These results suggest that the total score is a valid measure of emotional distress, so that the Italian version of HADS can be used as a screening questionnaire for psychiatric disorders. The use of the two subscales as a 'case identifier' or as an outcome measure should be considered with caution.
The productive replication of human immunodeficiency virus type 1 (HIV-1) occurs exclusively in defined cells of human or chimpanzee origin, explaining why heterologous animal models for HIV replication, pathogenesis, vaccination, and therapy are not available. This lack of an animal model for HIV-1 studies prompted us to examine the susceptibility of feline cells in order to evaluate the cat (Felis catus) as an animal model for studying HIV-1. Here, we report that feline cell lines harbor multiple restrictions with respect to HIV-1 replication. The feline CD4 receptor does not permit virus infection. Feline T-cell lines MYA-1 and FeT-1C showed postentry restrictions resulting in low HIV-1 luciferase reporter activity and low expression of viral Gag-Pol proteins when pseudotyped vectors were used. Feline fibroblastic CrFK and KE-R cells, expressing human CD4 and CCR5, were very permissive for viral entry and HIV-long terminal repeat-driven expression but failed to support spreading infection. KE-R cells displayed a profound block with respect to release of HIV-1 particles. In contrast, CrFK cells allowed very efficient particle production; however, the CrFK cellderived HIV-1 particles had low specific infectivity. We subsequently identified feline apolipoprotein B-editing catalytic polypeptide 3 (feAPOBEC3) proteins as active inhibitors of HIV-1 particle infectivity. CrFK cells express at least three different APOBEC3s: APOBEC3C, APOBEC3H, and APOBEC3CH. While the feAPOBEC3C did not significantly inhibit HIV-1, the feAPOBEC3H and feAPOBEC3CH induced G to A hypermutations of the viral cDNA and reduced the infectivity ϳ10-to ϳ40-fold.Like many retroviruses, human immunodeficiency virus type 1 (HIV-1) has a very limited host range; spreading replication is seen only in Homo sapiens and by artificial inoculation in the close relative the chimpanzee (Pan troglodytes) (2, 16), preventing the setup of an efficient small animal model for HIV-1 research. Many reasons argue against the widespread use of chimpanzees in research, including the ethical problems involved in the use of an endangered species, budgetary problems, and the very low induction of simian AIDS either from HIV-1 or its ancestor simian immunodeficiency virus cpz (SIVcpz) in infected chimpanzees (25,26,30,57,58,60,63).In general, the tropism of HIV-1 in human tissue is determined by the expression of its receptor protein CD4 together with CCR5 or CXCR4 chemokine receptors. Simian CD4 but not murine CD4 supports entry of HIV-1 (15, 33). HIV-1 entry through receptor-mediated membrane fusion is required for reverse transcription of the viral genomic RNA into a doublestranded DNA molecule. Murine T cells show early postentry restriction of HIV-1 at reverse transcription (3). In simian cells, a related restriction of HIV-1, but not of SIVs (5, 10, 53), involves the simian TRIM5␣ protein, which leads to increased viral uncoating and thereby suppresses reverse transcription (73). Since HIV-1 does not show spreading replication in nonhuman cells, cell type-and t...
The feline homologue of CD134 is the primary binding receptor for feline immunodeficiency virus (FIV), targeting the virus preferentially to activated CD4؉ helper T cells. However, strains of FIV differ in utilization of CD134; the prototypic strain PPR requires a minimal determinant in the first cysteine-rich domain (CRD1) of feline CD134 to confer near-optimal receptor function, while strains such as GL8 require additional determinants in the CD134 CRD2. We map this determinant to a loop in CRD2 governing the interaction between the receptor and its ligand; the amino acid substitutions S78N-S79Y-K80E restored full viral receptor activity to the CDR2 of human CD134 in the context of feline CD134, with tyrosine-79 appearing to be the critical residue for restoration of receptor function.The initial event in the process of virus entry into a target cell is the interaction between the virus and its cellular receptor; the specificity of this interaction determines both the cell tropism and the pathogenicity of the virus. The primary receptor for feline immunodeficiency virus (FIV) is CD134 (OX40) (13), a member of the tumor necrosis factor receptor (TNFR)/ nerve growth factor receptor family of molecules. CD134 expression is greatest on activated CD4 ϩ T-helper cells (7); thus, infection results in a progressive depletion of T-helper cells and AIDS-like illness. Primary isolates of FIV use CD134 as the binding receptor in conjunction with the chemokine receptor CXCR4 as a cofactor for infection (11,13,15). FIV binds specifically to CD134-expressing cells (13); FIV Env interacts directly with CD134 (4), and pretreatment of virus with soluble CD134 facilitates infection of CD134 Ϫ /CXCR4 ϩ cells (3). The binding site for the PPR strain of FIV has been mapped to the first cysteine-rich domain (CRD1) (3); human CD134 is not a functional receptor for FIV (13), and substitution of CRD1 of human CD134 with that of feline CD134 renders the molecule functional as a receptor for the PPR strain of FIV. However, expression of feline CD134 CRD1 in the context of human CD134 is insufficient to confer receptor function on many primary strains of FIV; additional determinants in CRD2 of feline CD134 are required to restore function (16), indicating differential utilization of CD134 by diverse strains of FIV (16). In order to map the determinants in CRD2, we compared the amino acid sequences of the CRD2s of feline and human CD134 (previously we identified the fragment spanning amino acids 65 to 82 as containing the critical determinant [s] [16]) and identified amino acid sequence differences (Fig. 1B). Next, using the human CRD2-containing chimera FFHH as our template, we proceeded to mutate the remaining amino acids in CRD2 from the human sequence to the feline sequence by PCR amplification from the FFHH template by using a mutagenic internal oligonucleotide (3Ј) carrying a BsrGI restriction site and a nonmutagenic external flanking (5Ј) primer carrying a BamHI restriction site. The following mutations were introduced: R66L-P67Q (...
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