RESUMEN
E2, along with E(rns) and E1, is an envelope glycoprotein of Classical Swine Fever Virus (CSFV). E2 is involved in several virus functions: cell attachment, host range susceptibility and virulence in natural hosts. Here we evaluate the role of a specific E2 region, (818)CPIGWTGVIEC(828), containing a putative fusion peptide (FP) sequence. Reverse genetics utilizing a full-length infectious clone of the highly virulent CSFV strain Brescia (BICv) was used to evaluate how individual amino acid substitutions within this region of E2 may affect replication of BICv. A synthetic peptide representing the complete E2 FP amino acid sequence adopted a ß-type extended conformation in membrane mimetics, penetrated into model membranes, and perturbed lipid bilayer integrity in vitro. Similar peptides harboring amino acid substitutions adopted comparable conformations but exhibited different membrane activities. Therefore, a preliminary characterization of the putative FP (818)CPIGWTGVIEC(828) indicates a membrane fusion activity and a critical role in virus replication.
Asunto(s)
Virus de la Fiebre Porcina Clásica/fisiología , Proteínas del Envoltorio Viral/metabolismo , Internalización del Virus , Sustitución de Aminoácidos , Animales , Línea Celular , Membrana Celular/metabolismo , Virus de la Fiebre Porcina Clásica/genética , Liposomas/metabolismo , Modelos Moleculares , Proteínas Mutantes/química , Proteínas Mutantes/genética , Proteínas Mutantes/metabolismo , Conformación Proteica , Genética Inversa , Porcinos , Proteínas del Envoltorio Viral/química , Proteínas del Envoltorio Viral/genéticaRESUMEN
Health care reform is also occurring in Australia and effects hospital chaplaincy programs. "Economic rationalism" is the philosophic foundation of this effort and its contrast with the values inherit in hospital chaplaincy are highlighted. Selected research results from the Australian system are described and the authors offer a perspective on the cost efficiency of hospital chaplaincy.