RESUMEN
Benefits of belatacept-based immunosuppressive regimens in human immunodeficiency virus (HIV)-positive renal transplant recipients include avoidance of drug interactions between calcineurin inhibitors and highly active antiretroviral agents and decreased likelihood or severity of nonimmune toxicities such as new-onset diabetes after transplant, hyperlipidemia and hypertension. We report a successful case of de novo belatacept at >18 mo from transplant in an HIV-positive black man aged 50 years who received his first transplant from a living related kidney donor. To our knowledge, this case is the first reported of belatacept use in an HIV-positive renal transplant recipient.
Asunto(s)
Abatacept/uso terapéutico , Rechazo de Injerto/tratamiento farmacológico , Supervivencia de Injerto/efectos de los fármacos , Infecciones por VIH/cirugía , Fallo Renal Crónico/cirugía , Trasplante de Riñón , Tasa de Filtración Glomerular , Rechazo de Injerto/epidemiología , Infecciones por VIH/virología , Seropositividad para VIH , VIH-1/aislamiento & purificación , Humanos , Inmunosupresores/uso terapéutico , Fallo Renal Crónico/virología , Pruebas de Función Renal , Masculino , Persona de Mediana Edad , Pronóstico , Receptores de TrasplantesRESUMEN
In the Gram-negative enterobacterium Erwinia (Pectobacterium) and Serratia sp. ATCC 39006, intrinsic resistance to the carbapenem antibiotic 1-carbapen-2-em-3-carboxylic acid is mediated by the CarF and CarG proteins, by an unknown mechanism. Here, we report a high-resolution crystal structure for the Serratia sp. ATCC 39006 carbapenem resistance protein CarG. This structure of CarG is the first in the carbapenem intrinsic resistance (CIR) family of resistance proteins from carbapenem-producing bacteria. The crystal structure shows the protein to form a homodimer, in agreement with results from analytical gel filtration. The structure of CarG does not show homology with any known antibiotic resistance proteins nor does it belong to any well-characterised protein structural family. However, it is a close structural homologue of the bacterial inhibitor of invertebrate lysozyme, PliI-Ah, with some interesting structural variations, including the absence of the catalytic site responsible for lysozyme inhibition. Both proteins show a unique ß-sandwich fold with short terminal α-helices. The core of the protein is formed by stacked anti-parallel sheets that are individually very similar in the two proteins but differ in their packing interface, causing the splaying of the two sheets in CarG. Furthermore, a conserved cation binding site identified in CarG is absent from the homologue.
Asunto(s)
Proteínas Bacterianas/química , Erwinia/química , Secuencia de Aminoácidos , Antibacterianos/farmacología , Proteínas Bacterianas/metabolismo , Sitios de Unión , Carbapenémicos/farmacología , Cationes/metabolismo , Cristalografía por Rayos X , Farmacorresistencia Bacteriana , Erwinia/efectos de los fármacos , Modelos Moleculares , Datos de Secuencia Molecular , Conformación Proteica , Multimerización de Proteína , Alineación de SecuenciaRESUMEN
Transplant pharmacists have been recognized as an essential part of the transplant team by their colleagues along with several governing and professional organizations. The specific education, training and responsibilities of the transplant pharmacist have not been clearly delineated in the literature. Various pharmacists across the country have been called upon to serve on the transplant team necessitating standardization of their fundamental and desirable activities. Therefore, the purpose of this manuscript is to describe the training and role of a transplant pharmacist on the patient care team and provide a roadmap to implementation of novel transplant pharmacy services.
