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PubMed1994

Identification of sperm antigen targets for immunocontraception: B-cell epitope analysis of Sp17.

The selection of immunological targets present on gametes is an important first step in the successful production of animal or human vaccines for immunocontraception. One strategy with regard to sperm antigens is to select antigens with physiological roles in gamete interaction, obtain the mRNA sequence for such an antigen, and then determine which region or domain of the molecule is available to the immune system when spermatozoa are presented to the female reproductive system. To illustrate this strategy, we have used the rabbit sperm antigen Sp17 (RSA-3), which has been cloned and sequenced. The peptide pin-block method of Chiron Mimotopes, Australia, has been used to analyse the 146 amino acids of Sp17 with various homologous and heterologous antisera. This study demonstrates that such an analysis can lead to the identification of a B-cell epitope with strong immunocontraceptive potential.

Amino Acid Sequence↗
PubMed2006

Sog/Chordin is required for ventral-to-dorsal Dpp/BMP transport and head formation in a short germ insect.

Bone morphogenetic protein (BMP) signaling plays a major role in dorsoventral patterning in vertebrates and in Drosophila. Remarkably, in Tribolium, a beetle with an ancestral type of insect development, early BMP/dpp exhibits differential expression along the anteroposterior axis. However, the BMP/Dpp inhibitor Sog/chordin is expressed ventrally and establishes a dorsal domain of BMP/Dpp activity by transporting BMPs toward the dorsal side, like in Drosophila. Loss of Tribolium Sog not only abolishes dorsoventral polarity in the ectoderm, but also leads to the complete absence of the CNS. This phenotype suggests that sog is the main BMP antagonist in Tribolium, in contrast to vertebrates and Drosophila, which possess redundant antagonists. Surprisingly, Sog also is required for head formation in Tribolium, as are the BMP antagonists in vertebrates. Thus, in Tribolium, the system of BMP and its antagonists is less complex than in Drosophila or vertebrates and combines features from both, suggesting that it might represent an ancestral state.

Animals↗
PubMed1985

Molecular cloning, cDNA sequencing, and chemical synthesis of cecropin B from Hyalophora cecropia.

Two cDNA clones containing coding information for cecropin B from the Cecropia moth (Hyalophora cecropia) were identified by means of a synthetic probe. Sequencing of the two inserts showed that cecropin B is processed from a 62-amino acid residue precursor molecule including a 26-residue leader peptide and a COOH-terminal glycine residue. The latter presumably donates the nitrogen of the amide group present on the COOH-terminal leucine residue of the mature cecropin B. The sequence deduced for the mature cecropin B differed in the COOH-terminal region from the tentative structure previously determined by carboxypeptidase digestion. To settle the discrepancy, cecropin B was synthesized according to the cDNA sequence with an amidated COOH-terminal leucine. Natural and synthetic cecropin B were found to be indistinguishable with respect to electrophoretic mobility and antibacterial activity against seven different bacteria. The COOH-terminal tetrapeptides were isolated from both natural and synthetic cecropin B and found to be indistinguishable. The correct sequence for cecropin B is (formula; see text).

Amino Acid Sequence↗
PubMed1988

Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes.

Cecropins, positively charged antibacterial peptides found in the cecropia moth, and synthetic peptide analogs form large time-variant and voltage-dependent ion channels in planar lipid membranes in the physiological range of concentration. Single-channel conductances of up to 2.5 nS (in 0.1 M NaCl) were observed, which suggests a channel diameter of 4 nm. Channels formed by the peptides cecropin AD and MP3 had a permeability ratio of Cl-/Na+ = 2:1 in 0.1 M NaCl. A comparative study of the three cecropins, cecropins A, B, and D, and of six synthetic analogs allowed determination of structural requirements for pore formation. Shorter amphipathic peptides did not form channels, although they adsorbed to the bilayer. A flexible segment between the N-terminal amphipathic region and the C-terminal more hydrophobic region of the peptide was required for the observation of a time-variant, voltage-dependent conductance. Cecropin AD was the most effective voltage-dependent pore-forming peptide and was also the most potent antibacterial peptide against several test organisms. A positive surface charge or cholesterol in the bilayer reduced the conductances caused by cecropin AD or MP3 by at least 5-fold. This behavior is consistent with the known insensitivity of eukaryotic cells to cecropins. Our observations suggest that the broad antibacterial activity of cecropins is due to formation of large pores in bacterial cell membranes.

Amino Acid Sequence↗
PubMed1988

Characterization and cDNA cloning of the pheromone-binding protein from the tobacco hornworm, Manduca sexta: a tissue-specific developmentally regulated protein.

cDNA encoding pheromone-binding protein (PBP), the major soluble protein in olfactory sensilla of male moths, has been cloned from the tobacco hornworm, Manduca sexta. A study of the developmental time course of PBP reveals that it is first synthesized just prior to eclosion and that the percentage of antennal mRNA encoding PBP shifts from zero to about 20% at that time. PBP is also found in sensilla from female M. sexta antennae. No amino acid sequence homology is observed between PBP and the vertebrate odorant-binding protein.

Amino Acid Sequence↗
PubMed1990

Parasitoid virus-like particles destroy Drosophila cellular immunity.

Parasitoid wasps must avoid the destructive effects of the host's cellular defense system in order to exploit the host hemocoel as a suitable environment for their survival. To protect their eggs from encapsulation by Drosophila melanogaster blood cells, Leptopilina heterotoma females inject a factor that selectively destroys lamellocytes, the type of Drosophila blood cell involved in recognition and encapsulation of large foreign objects. Other types of host blood cells, including the phagocytic plasmatocytes, remain functional. This report demonstrates that the destructive factor for lamellocytes is a virus-like particle (VLP) stored in the reservoir of an accessory gland associated with the female wasp reproductive system. We show that VLPs enter Drosophila blood cells in vitro. VLPs are found free in the cytoplasm of lamellocytes but are confined to phagocytic vesicles of plasmatocytes. As lamellocytes are susceptible to the VLP infection and plasmatocytes are not, we conclude that the mode of VLP entry and its disposition in the cytoplasm determine the fate of the infected host blood cell.

Animals↗
PubMed1991

Molecular cloning and analysis of small optic lobes, a structural brain gene of Drosophila melanogaster.

Mutations in the small optic lobes (sol) gene of Drosophila melanogaster cause specific cells to degenerate in the developing optic lobes, resulting in the absence of certain classes of columnar neurons. These neuronal defects lead to specific alterations in behavioral characteristics, particularly during flight and walking maneuvers. We have isolated the wild-type sol locus by microcloning and chromosomal walking and have established its genetic and molecular limits. Two major transcripts of 5.8 and 5.2 kilobases are produced from this locus by alternative splicing and are present throughout the entire life cycle. Sequence analyses of cDNAs corresponding to these two classes of transcripts predict two proteins of 1597 and 395 amino acids. The first shows similarity in its carboxyl-terminal region to the catalytic domain of a vertebrate calcium-activated neutral protease (calpain), whereas its amino-terminal region contains several zinc-finger-like repeats of the form WXCX2CX10-11CX2C. The second predicted protein contains only the first two of the zinc-finger-like repeats and is missing the calpain domain. By constructing transgenic flies carrying a single wild-type copy of the sol gene in a homozygous sol mutant background, we have restored the normal neuroanatomical phenotype to individuals that would have developed mutant brains.

Amino Acid Sequence↗
PubMed1992

Molecular characterization and silk gland expression of Bombyx engrailed and invected genes.

Genetic analysis in Drosophila has shown that engrailed (en) plays an important role in segmentation and neurogenesis. A closely related gene, invected (in), is coexpressed with en in the posterior developmental compartments where en is known to specify cell state. We report here the isolation of two en-like cDNAs from the middle silk glands of Bombyx mori larvae. Sequence analysis revealed that they are the counterparts of Drosophila en and in. Four highly conserved domains, including the homeodomain, were identified in these En and In proteins from Bombyx and Drosophila. In addition, two en-specific and one in-specific domains could also be found. These structurally homologous genes might share a similar role in Bombyx development. They were found to be coexpressed in the middle silk gland but not in the posterior silk gland during the fourth molt/fifth intermolt period. We speculate that these Bombyx en-like genes might be involved in the compartmentalization of the silk gland.

Amino Acid Sequence↗
PubMed1992

Cloning of Drosophila transcription factor Adf-1 reveals homology to Myb oncoproteins.

The Drosophila sequence-specific DNA binding protein, Adf-1, is capable of activating transcription of the alcohol dehydrogenase gene, Adh, and is implicated in the transcriptional control of other developmentally regulated genes. We have cloned the cDNA encoding Adf-1 by generating specific DNA probes deduced from partial amino acid sequence of the protein. Several cDNA clones encoding an extended open reading frame were isolated from a phage lambda library. The complete amino acid sequence of Adf-1 deduced from the longest cDNA reveals structural similarities to the putative helix-turn-helix DNA binding motif of Myb and Myb-related proteins. DNA sequence analysis of genomic clones and Northern blot analysis of mRNA suggest that Adf-1 is a single-copy gene encoding a 1.9-kb transcript. Purified recombinant Adf-1 expressed in Escherichia coli binds specifically to Adf-1 recognition sites and activates transcription of a synthetic Adh promoter in vitro in a manner indistinguishable from the protein purified from Drosophila. Temporally staged Drosophila embryos immunochemically stained with affinity-purified anti-Adf-1 antibodies indicate that Adf-1 protein is not detectable in very early embryos and does not appear to be maternally inherited. During later stages of embryogenesis, Adf-1 appears to be expressed in the nucleus of most somatic cells in the embryo with possibly higher concentrations found in some tissues.

Alcohol Dehydrogenase↗
PubMed1993

Role of the integument in insect immunity: epicuticular abrasion and induction of cecropin synthesis in cuticular epithelial cells.

When the epicuticle of a silkworm larva, Bombyx mori, was lightly abraded in the presence of live Bacillus licheniformis, Enterobacter cloacae, or bacterial cell wall components, cecropin mRNAs were detected in the underlying epithelial cells and in fat body cells remote from the abraded area. Antibacterial activity due to cecropin was detected in the matrix of the lightly abraded cuticle but not in nonabraded portions of the cuticular matrix or in the hemolymph surrounding the fat body, unless a more severe cuticular abrasion was administered. A light abrasion to a larva of the giant silkworm moth, Hyalophora cecropia, in the presence of E. cloacae also induced antibacterial activity in the abraded cuticle. These data illustrate that the ectodermally derived lepidopteran larval integument, when challenged by live bacteria or their cell wall components, mounts an immune response. Hence, the insect exoskeleton, which is often considered as an inert protective armor, is indeed actively participating in defense.

Animals↗
PubMed1993

Calphotin: a Drosophila photoreceptor cell calcium-binding protein.

Monoclonal antibody 23E9 identifies a calcium-binding protein, calphotin, in photoreceptor cells of the Drosophila melanogaster compound eyes and ocelli. The antigen is restricted to a defined cytoplasmic region; it is not present in the rhabdomeres, nuclei, mitochondria, or rough endoplasmic reticulum. A corresponding cDNA recognizes a 3-kb mRNA with retinal specificity similar to the antigen and maps to band 86E/F-87A/B on chromosome 3. An open reading frame of 2595 bp encodes an estimated 85-kDa protein of unusual amino acid composition, with > 50% proline, alanine, and valine and very few basic residues. The C-terminal segment contains a leucine zipper motif uninterrupted by prolines. We found no significant similarities with the GenBank or National Biomedical Resource Foundation data bases. The location of the protein within a distinct cytoplasmic region suggests that it might function as a calcium-sequestering "sponge" to regulate the amount of free cytoplasmic calcium.

Amino Acid Sequence↗
PubMed1993

A Drosophila photoreceptor cell-specific protein, calphotin, binds calcium and contains a leucine zipper.

The calphotin protein, encoded by the calphotin (cap) gene, is expressed in the soma and axons of all Drosophila photoreceptor cells. It is expressed early in photo-receptor cell development, at the time when cell-type decisions are being made. Expression of calphotin is not altered by the glass mutation, which blocks photoreceptor cell development. The calphotin protein binds calcium and contains a long C-terminal leucine zipper. Potential implications of these properties are discussed.

Amino Acid Sequence↗
PubMed1995

A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense.

In this paper we report a recessive mutation, immune deficiency (imd), that impairs the inducibility of all genes encoding antibacterial peptides during the immune response of Drosophila. When challenged with bacteria, flies carrying this mutation show a lower survival rate than wild-type flies. We also report that, in contrast to the antibacterial peptides, the antifungal peptide drosomycin remains inducible in a homozygous imd mutant background. These results point to the existence of two different pathways leading to the expression of two types of target genes, encoding either the antibacterial peptides or the antifungal peptide drosomycin.

Animals↗
PubMed1995

TRPC1, a human homolog of a Drosophila store-operated channel.

In many vertebrate and invertebrate cells, inositol 1,4,5-trisphospate production induces a biphasic Ca2+ signal. Mobilization of Ca2+ from internal stores drives the initial burst. The second phase, referred to as store-operated Ca2+ entry (formerly capacitative Ca2+ entry), occurs when depletion of intracellular Ca2+ pools activates a non-voltage-sensitive plasma membrane Ca2+ conductance. Despite the prevalence of store-operated Ca2+ entry, no vertebrate channel responsible for store-operated Ca2+ entry has been reported. trp (transient receptor potential), a Drosophila gene required in phototransduction, encodes the only known candidate for such a channel throughout phylogeny. In this report, we describe the molecular characterization of a human homolog of trp, TRPC1. TRPC1 (transient receptor potential channel-related protein 1) was 40% identical to Drosophila TRP over most of the protein and lacked the charged residues in the S4 transmembrane region proposed to be required for the voltage sensor in many voltage-gated ion channels. TRPC1 was expressed at the highest levels in the fetal brain and in the adult heart, brain, testis, and ovaries. Evidence is also presented that TRPC1 represents the archetype of a family of related human proteins.

Adult↗
PubMed1996

Common endocrine and genetic mechanisms of behavioral development in male and worker honey bees and the evolution of division of labor.

Temporal polyethism is a highly derived form of behavioral development displayed by social insects. Hormonal and genetic mechanisms regulating temporal polyethism in worker honey bees have been identified, but the evolution of these mechanisms is not well understood. We performed three experiments with male honey bees (drones) to investigate how mechanisms regulating temporal polyethism may have evolved because, relative to workers, drones display an intriguing combination of similarities and differences in behavioral development. We report that behavioral development in drones is regulated by mechanisms common to workers. In experiment 1, drones treated with the juvenile hormone (JH) analog methoprene started flying at significantly younger ages than did control drones, as is the case for workers. In experiment 2, there was an age-related increase in JH associated with the onset of drone flight, as in workers. In experiment 3, drones derived from workers with fast rates of behavioral development themselves started flying at younger ages than drones derived from workers with slower rates of behavioral development. These results suggest that endocrine and genetic mechanisms associated with temporal polyethism did not evolve strictly within the context of worker social behavior.

Aging↗
PubMed1999

Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold.

We demonstrate that the ligand pocket of a lipocalin from Pieris brassicae, the bilin-binding protein (BBP), can be reshaped by combinatorial protein design such that it recognizes fluorescein, an established immunological hapten. For this purpose 16 residues at the center of the binding site, which is formed by four loops on top of an eight-stranded beta-barrel, were subjected to random mutagenesis. Fluorescein-binding BBP variants were then selected from the mutant library by bacterial phage display. Three variants were identified that complex fluorescein with high affinity, exhibiting dissociation constants as low as 35.2 nM. Notably, one of these variants effects almost complete quenching of the ligand fluorescence, similarly as an anti-fluorescein antibody. Detailed ligand-binding studies and site-directed mutagenesis experiments indicated (i) that the molecular recognition of fluorescein is specific and (ii) that charged residues at the center of the pocket are responsible for tight complex formation. Sequence comparison of the BBP variants directed against fluorescein with the wild-type protein and with further variants that were selected against several other ligands revealed that all of the randomized amino acid positions are variable. Hence, a lipocalin can be used for generating molecular pockets with a diversity of shapes. We term this class of engineered proteins "anticalins." Their one-domain scaffold makes them a promising alternative to antibodies to create a stable receptor protein for a ligand of choice.

Amino Acid Sequence↗
PubMed1995

cDNA sequence and expression of the ceratotoxin gene encoding an antibacterial sex-specific peptide from the medfly Ceratitis capitata (diptera).

Ceratotoxins are antibacterial 3-kDa molecular mass amphiphilic peptides isolated from the female reproductive accessory glands of the medfly Ceratitis capitata. They are physiologically related to bee melittin and show amino acid sequence homology with magainin peptides. In this paper, we report the complete sequence of cDNA coding for ceratotoxin A and the expression of the gene during the life cycle of the insect. Experimental data show that the ceratotoxin is a gene expressed exclusively in the imaginal stages and that it is female-specific, related to sexual maturity, and stimulated by mating. Differently from most antibacterial insect hemolymph peptides, it is not induced by microbial infection. Western blot analysis using an anti-ceratotoxin antibody indicates the female accessory glands as the only site where the production of the ceratotoxin peptide occurs.

Amino Acid Sequence↗
PubMed1995

Serine protease inhibition by insect peptides containing a cysteine knot and a triple-stranded beta-sheet.

Three insect peptides showing high sequence similarity and belonging to the same structural family incorporating a cysteine knot and a short three-stranded antiparalled beta-sheet were studied. Their inhibitory effect on two serine proteases (bovine alpha-chymotrypsin and human leukocyte elastase) is reported. One of them, PMP-C, is a strong alpha-chymotrypsin inhibitor (Ki = 0.2 nM) and interacts with leukocyte elastase with a Ki of 0.12 microM. The other two peptides, PMP-D2 and HI, interact only weakly with alpha-chymotrypsin and do not inhibit leukocyte elastase. Synthetic variants of these peptides were prepared by solid-phase synthesis, and their action toward serine proteases was evaluated. This enabled us to locate the P1 residues within the reactive sites (Leu-30 for PMP-C and Arg-29 for PMP-D2 and HI), and, interestingly, variants of PMP-D2 and HI were converted into powerful inhibitors of both alpha-chymotrypsin and leukocyte elastase, the most potent elastase inhibitor obtained in this study having a Ki of 3 nM.

Amino Acid Sequence↗