RESUMEN
El constante desarrollo de las enfermedades infecciosas, conjuntamente con la aparición de la resistencia microbiana a los antibióticos, ha originado que nuevamente se piense en los fagos como opción terapéutica. De hecho, existe una importante aportación bibliográfica sobre los bacteriófagos y su utilidad para eliminar los procesos infecciosos, lo que ha justificado el continuar investigando acerca del posible uso de estos y de sus productos génicos, como esperanzadora alternativa a los tratamientos con antimicrobianos disponibles en la actualidad. Por ello, en este artículo se ofrece información sobre estos microorganismos, en específico sobre los enzibióticos, y se propone que sean considerados en el combate contra las infecciones bacterianas.
The constant development of the infectious diseases, together with the emergence of the microbial resistance to the antibiotics, has originated that again it is thought on the phages as therapeutic option. In fact, an important literature contribution exists about the bacteriophages and their use to eliminate infectious processes, what has justified the continuity in investigating about the possible use of them and of their genic products, as a promising alternative for treatments with antimicrobials currently available. That is why, information on these microorganisms is offered in this work, specifically on the enzibiotics, and is it intended them to be considered in the bacterial infections control.
Asunto(s)
Humanos , Masculino , Femenino , Infecciones Bacterianas/diagnóstico , Bacteriófagos/enzimología , Resistencia a Medicamentos , Enfermedades Transmisibles , Farmacorresistencia Microbiana , Peloterapia/métodosRESUMEN
φC31 integrase encoded by Streptomyces phage can mediate site-specific recombination between phage and host genomes. The recombination direction is generally considered to be accurately regulated, but the regulatory mechanisms involved are still unclear. Recently, some hyperactive mutants of φC31 integrase that can bypass the regulatory steps have been isolated and extensively studied. A putative coiled-coil region is found to play a critical role in controlling recombination direction. Further analysis led us to the speculation that at least two regions in the N-terminal domain of φC31 integrase are involved in the tetrameric interfaces and that the putative coiled coil interacts with one of the regions to regulate the recombination direction.
Asunto(s)
Bacteriófagos/enzimología , Integrasas/metabolismo , Recombinación Genética , Secuencia de Aminoácidos , Emparejamiento Cromosómico , Integrasas/química , Modelos Genéticos , Datos de Secuencia Molecular , Mutación/genética , Multimerización de Proteína , Estructura Terciaria de Proteína , Alineación de SecuenciaRESUMEN
Many gene therapy strategies require transfer of high-molecular weight DNA into human cells. To enable clinical trials, these vectors need to be produced on a large scale and at low cost. The production of effective high-capacity vectors like HSV-amplicons and helper-dependent adenoviral vectors is difficult to up-scale, so new inexpensive vectors are needed for the efficient delivery of high-molecular weight DNA to human cells. Bacteriophage lambda vectors can accommodate up to about 46 kb of therapeutic DNA and can be easily produced in an industrial setting. However, the lambda vectors transfer DNA into mammalian cells with only a low efficiency. It was shown that bacteriophage lambda virions ejected their DNA in the presence of the purified receptor for bacteriophage lambda, maltoporin (LamB protein), encoded by the malB gene of Shigella sonnei 3070. This property of S. sonnei maltoporin was exploited for the bacteriophage injection-driven DNA loading of liposomes and other polymer nanocontainers displaying maltoporin. Relying on the above evidence I hypothesize that the efficient gene transfer by industrially produced bacteriophage lambda vector virions, such as cosmid transducing particles, to human cells can be accomplished after incorporation (protein painting) of the purified S. sonnei maltoporin into the human plasma membrane.