RESUMO
Taste receptors are receptor proteins that detect ligands belonging to the 5 taste modalities: sweet, bitter, sour, salty, and umami. Taste receptors are not restricted to taste cells in taste buds; rather, they are distributed throughout the entire body. For example, solitary chemosensory cells (SCCs) and tuft cells express taste signal proteins and are present in several mucosae. In the airways, SCCs sense bacteria, allergens, viruses, and noxious stimuli and drive evasive behavior, neuroinflammation, and antibacterial responses. In the gut, tuft cells detect helminth infection and bacterial dysbiosis and initiate type II immune responses characterized by tissue remodeling. In the gingiva, SCCs detect oral pathogenic bacteria, evoke innate immune responses and release antimicrobial compounds in the epithelium, and regulate the microbiome composition. This review summarizes the most recent research on extragustatory taste receptors and their function in antibacterial defense. We also discuss how these findings have provided insights into the development of potential therapeutic strategies for mucosal bacterial infection and dental diseases.
Assuntos
Papilas Gustativas , Antibacterianos , Bactérias/metabolismo , Imunidade Inata , Saúde Bucal , Receptores Acoplados a Proteínas G/metabolismo , Paladar/fisiologia , Papilas Gustativas/metabolismoRESUMO
Canine distemper virus (CDV) is a pathogen which affects members of the Canidae family, causing an acute, often fatal, systemic disease. CDV is an RNA virus of the family Paramyxoviridae that contains two envelope glycoproteins: F and HA. In this study, we focused on the envelope glycoprotein F as the main target for neutralizing antibodies produced after infection or vaccination. The complete coding region of the protein (60 kDa) was expressed in the methylotrophic yeast Pichia pastoris, obtained in a recombinant form and secreted to the culture medium. Later, to analyze its immunogenicity, the protein was combined with an oily adjuvant and used to inoculate mice. The results provide evidence supporting a potential application of this recombinant protein as a subunit vaccine.
RESUMO
The effects of the biocide Triclosan, used in personal care products and known as a common environmental contaminant, on byssal apparatus were studied in the marine mussel Mytilus galloprovincialis. Experimental evidences indicated that an exposure for 7 days at a concentration of 10⯵g/L induced marked alterations in the byssus gland resulting in a significant delay in byssus regrowth and in a decrease in threads resistance to traction. Such alterations in animals exposed to tidal and waves action would cause a significant loss in ecological fitness and severely impact on mussel survival. Triclosan release in coastal environments therefore should be more carefully monitored to prevent drastic consequences.
Assuntos
Desinfetantes/toxicidade , Mytilus/fisiologia , Triclosan/toxicidade , Animais , Meio Ambiente , Mytilus/efeitos dos fármacos , Poluentes Químicos da ÁguaRESUMO
The glycoprotein (G-protein) of rabies virus is responsible for viral attachment to the host cell surface and induces virus neutralization antibodies. In the present study, the G-protein gene of rabies virus CVS strain was cloned, sequenced and expressed in the yeast, Pichia pastoris, as a secreted protein, using a simplified DO-stat control feeding strategy. This strategy involves the addition of methanol when the dissolved oxygen (DO) level rises above the setpoint avoiding methanol accumulation and oxygen limitation. The G-protein expression was evaluated by SDS-PAGE, ELISA, and western blot assays. Like native G-protein, the recombinant G-protein was found reactive when it was challenged against specific antibodies. The data indicate that the recombinant G-protein can be easily expressed and isolated, and may be useful as a safe source in the production of diagnostic kits and subunit vaccines to prevent rabies.
Assuntos
Pichia/metabolismo , Vírus da Raiva/genética , Proteínas do Envelope Viral , Pichia/genética , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Proteínas do Envelope Viral/biossíntese , Proteínas do Envelope Viral/química , Proteínas do Envelope Viral/genéticaRESUMO
This work reports a method for rapid amplification of the complete genome of equine influenza virus subtype 2 (H3N8). A ThermoScript reverse transcriptase instead of the avian myeloblastosis virus reverse transcriptase or Moloney murine leukemia virus reverse transcriptase was used. This enzyme has demonstrated higher thermal stability and is described as suitable to make long cDNA with a complex secondary structure. The product obtained by this method can be cloned, used in later sequencing reactions or nested-PCR with the purpose of achieving a rapid diagnosis and characterization of the equine influenza virus type A. This detection assay might be a valuable tool for diagnosis and screening of field samples as well as for conducting molecular studies.