Biomedical subjects

Richard G Vogt

Publications and source records attributed to Richard G Vogt.

5 recordsLinked to original sources

PubMed2006

How sensitive is a nose?

Odor sensitivity may not be due to odor-receptor (OR) binding but rather may be due to emergent properties of transduction pathways and the anatomical convergence of olfactory neurons. A recent study suggests that odor-OR interactions are brief and infrequently activate heterotrimeric GTP-binding proteins (G proteins); in contrast, visual receptors have long-lasting activation states and activate many G proteins. These differences may reflect strategies that evolved to accommodate very different signals, and the mechanisms described might be applicable for receptors across phyla. However, whereas visual receptors (rhodopsin) appeared before protostome-deuterostome separation, ORs may be independently derived in different phyla. Alternatively, phylum-distinct ORs may share common ancestry but be influenced by diversifying selection. Phylum-distinct ORs may imply phylum-specific OR mechanisms, whereas common ancestry may imply common mechanisms. Nonetheless, most animals detect a similar repertoire of olfactory signals, and OR mechanisms may be convergent on those signals independent of receptor relatedness. Thus, recent insights into the molecular characteristics of odor perception in frogs may well be relevant to such processes as how mosquitoes detect host odors for a malaria-transmitting blood meal.

Animals↗

PubMed2005

Antennal expressed genes of the yellow fever mosquito (Aedes aegypti L.); characterization of odorant-binding protein 10 and takeout.

A small cDNA library was constructed from antennae of 100 adult male Aedes aegypti yellow fever mosquitoes. Sequencing of 80 clones identified 49 unique gene products, including a member of the Odorant Binding Protein family (Aaeg-OBP10), a homologue of Takeout (Aaeg-TO), and transposable elements of the LINE, SINE and MITE classes. Aaeg-OBP10 encodes a 140 amino acid protein including a predicted 25 amino acid signal peptide. Aaeg-OBP10 expression was adult male enriched, increased with adult age, and greatest in antennae and wings but also present in maxillary palps, proboscis and leg. Aaeg-OBP10 is a likely orthologue of Agam-OBP10 of the malaria mosquito Anopheles gambiae and shares significant similarity with members of the OBP56 gene cluster of Drosophila melanogaster. These OBP genes may represent a unified class of OBPs with unique roles in chemodetection; the expression pattern of Aaeg-OBP10 suggests it may play a role in adult male chemosensory behavior. Aaeg-TO encodes a 248 amino acid protein including a predicted 22 amino acid signal peptide. Aaeg-TO is homologous with the circadian/feeding regulated D. melanogaster Takeout protein (Dmel-TO) and a subclass of Juvenile Hormone Binding Proteins (JHBP) characterized by Moling from Manduca sexta; both Dmel-TO and Moling are sensitive to feeding, suggesting Aaeg-TO might regulate the antennal response to food, host or pheromonal odors in a JH sensitive manner. Aaeg-TO was used to identify 25 D. melanogaster and 13 A. gambiae homologues by Blast analysis suggesting these may comprise a relatively large class of protein involved in the hormonal regulation of behavior.

Aedes↗

PubMed2004

Behavioral responses of newly hatched zebrafish (Danio rerio) to amino acid chemostimulants.

The zebrafish chemosensory systems of olfaction, taste and solitary chemosensory cells (SCCs) are established during the first week after fertilization (a.f.). These systems presumably support the early development of feeding behaviors required as yolk supplies diminish over the same period. Yet there is no previous data reporting early chemosensory responses in zebrafish. We therefore assayed the chemosensory behavior of newly hatched zebrafish on days 3, 4 and 5 a.f. Responses were compared between fish exposed to water alone versus water containing a mixture of 12 amino acids (100 microM each) flowing through a 50 ml test chamber at 4 ml/min; computer-assisted motion analysis was used to quantify responses. Behavioral responses were first observed at day 4 a.f.; the number of fish swimming, their swimming speeds, and their net-to-gross displacement (NGDR) all increased significantly in response to amino acid stimulation. Because taste buds first appear 4-5 days a.f. and the SCCs may not respond to amino acids, these initial chemosensory responses of day 4 fish may be mediated by already established olfactory neurons. The onset of chemosensitivity in day 4 fish corresponded with an easily recognizable developmental phenotype of inactive floating; day 3 fish were inactive and resting on the bottom while day 5 fish were active and moving through the water column. The ease of identifying responsive day 4 fish suggests these animals may be useful for characterizing odorant sensitivity or developmental plasticity or for screening for chemosensory mutations.

Amino Acids↗

PubMed2002

Odorant binding protein homologues of the malaria mosquito Anopheles gambiae; possible orthologues of the OS-E and OS-F OBPs OF Drosophila melanogaster.

Twenty-nine Anopheles gambiae candidate Odorant Binding Proteins (OBPs) were characterized for similarity to OBPs of Drosophila melanogaster and other insects. Twenty-five of these sequences were identified by BLAST searching the A. gambiae genome database. Several A. gambiae sequences were significantly similar to the D. melanogaster OBPs OS-E/OS-F, LUSH and PBPRP2/PBPRP5. Exon boundary comparisons suggests that two A. gambiae genes are orthologues of OS-E and OS-F, justifying the names AgamOS-E (EAA0 1090, AF437886) and AgamOS-F (EAA14641, AF437884). If these are orthologues. then the gene duplication establishing the OS-E and OS-F lineages predated the divergence of mosquitoes and flies. The identification of orthologous OBPs and other chemosensory genes between D. melanogaster and A. gambiae should accelerate the transfer of physiological and behavioral information between these two species.

Animals↗

PubMed2002

A comparative study of odorant binding protein genes: differential expression of the PBP1-GOBP2 gene cluster in Manduca sexta (Lepidoptera) and the organization of OBP genes in Drosophila melanogaster (Diptera).

Insects discriminate odors using sensory organs called olfactory sensilla, which display a wide range of phenotypes. Sensilla express ensembles of proteins, including odorant binding proteins (OBPs), olfactory receptors (ORs) and odor degrading enzymes (ODEs); odors are thought to be transported to ORs by OBPs and subsequently degraded by ODEs. These proteins belong to multigene families. The unique combinatorial expression of specific members of each of these gene families determines, in part, the phenotype of a sensillum and what odors it can detect. Furthermore, OBPs, ORs and ODEs are expressed in different cell types, suggesting the need for cell-cell communication to coordinate their expression. This report examines the OBP gene family. In Manduca sexta, the genes encoding PBP1Msex and GOBP2Msex are sequenced, shown to be adjacent to one another, and characterized together with OBP gene structures of other lepidoptera and Drosophila melanogaster. Expression of PBP1Msex, GOBP1Msex and GOBP2Msex is characterized in adult male and female antenna and in larval antenna and maxilla. The genomic organization of 25 D. melanogaster OBPs are characterized with respect to gene locus, gene cluster, amino acid sequence similarity, exon conservation and proximity to OR loci, and their sequences are compared with 14 M. sexta OBPs. Sensilla serve as portals of important behavioral information, and genes supporting sensilla function are presumably under significant evolutionary selective pressures. This study provides a basis for studying the evolution of the OBP gene family, the regulatory mechanisms governing the coordinated expression of OBPs, ORs and ODEs, and the processes that determine specific sensillum phenotypes.

Amino Acid Sequence↗