RESUMO
Coccidioides immitis is a dimorphic fungus that grows as a filamentous mold in soil and as a spherule at human body temperature. The hyphal or soil form is found rarely in human tissue. We report 5 cases of coccidioidomycosis in which hyphae were found in brain tissue or spinal fluid. The presence of central nervous system plastic devices appears to be associated with morphological reversion to the saprophytic form. This reversion has implications for diagnosis and therapy and may increase the risk of obstruction of the device(s).
Assuntos
Encefalopatias/diagnóstico , Encéfalo/microbiologia , Coccidioides/classificação , Coccidioidomicose/diagnóstico , Derivação Ventriculoperitoneal/efeitos adversos , Adulto , Antifúngicos/uso terapêutico , Encefalopatias/tratamento farmacológico , Encefalopatias/etiologia , Coccidioides/isolamento & purificação , Coccidioidomicose/líquido cefalorraquidiano , Coccidioidomicose/tratamento farmacológico , Coccidioidomicose/etiologia , Evolução Fatal , Feminino , Humanos , Masculino , Testes de Sensibilidade Microbiana , Pessoa de Meia-Idade , Prognóstico , Medição de RiscoRESUMO
Strains of vancomycin-resistant enterococci (VRE) have emerged and spread widely throughout the United States during the last few years. Multiply-resistant strains of Enterococcus faecium are especially troublesome because they are often resistant to all commercially available antimicrobial agents. At present, VRE infections occur most often in hospitalized patients with severe underlying disease who have undergone invasive procedures and received prolonged courses of broad-spectrum antimicrobial therapy. Because therapeutic options are limited, prevention of spread from patients with known cases to other vulnerable patients is essential.
Assuntos
Antibacterianos/farmacologia , Enterococcus faecalis/efeitos dos fármacos , Enterococcus faecium/efeitos dos fármacos , Infecções por Bactérias Gram-Positivas/tratamento farmacológico , Vancomicina/farmacologia , Antibacterianos/uso terapêutico , Infecção Hospitalar/tratamento farmacológico , Infecção Hospitalar/microbiologia , Infecção Hospitalar/transmissão , Resistência Microbiana a Medicamentos , Resistência a Múltiplos Medicamentos , Enterococcus faecalis/crescimento & desenvolvimento , Enterococcus faecium/crescimento & desenvolvimento , Infecções por Bactérias Gram-Positivas/transmissão , Humanos , Fatores de Risco , Vancomicina/uso terapêuticoRESUMO
A monoclonal antibody (mAb L6) to a carcinoma surface antigen has previously been shown to recognize neurophysins (NP), proteins associated with oxytocin and vasopressin. L6-reactivity in rat hypothalamus was confined to magnocellular neuronal systems. No staining was detected in parvicellular suprachiasmatic or paraventricular systems. mAb L6 immunoprecipitated vasopressin-neurophysin only under reducing conditions, and detected it in Western blots only after gel-renaturation and electroblotting in basic buffer. These findings suggest L6-reactivity to NP is conformation-sensitive, and imply NP expression in a unique configurational form in hypothalamic parvicellular systems.
Assuntos
Anticorpos Monoclonais , Hipotálamo/citologia , Neurônios/citologia , Neurofisinas/análise , Animais , Hipotálamo/química , Immunoblotting , Imuno-Histoquímica , Masculino , Eminência Mediana/citologia , Peso Molecular , RatosRESUMO
An immunoblotting method to detect low-molecular-weight peptides with monoclonal antibodies that normally fail to demonstrate immunoreactivity using conventional blotting techniques is described. Detection of neurophysin, insulin, calcitonin, vasopressin, and beta-endorphin electroblotted on nitrocellulose membranes was optimized after introducing four modifications into the conventional procedure. These include renaturing the gels after sodium dodecyl sulfate electrophoresis, electroblotting the renatured gels in basic transfer buffer, fixing and/or heating the blots, and using avidin/alkaline phosphatase conjugates for antigen/antibody detection. This technique likely enables the denatured peptides to regain their native conformation and, therefore, restores antigenicity and recognition by highly structural specific monoclonal antibodies. Although the most dramatic improvement with this technique is with monoclonal antibodies, a modest improvement in sensitivity can be obtained when immunoblots are probed with polyclonal antibodies. The high resolution of this system will be useful in probing blots of partial proteolytic digests of proteins with both monoclonal and polyclonal antibodies.