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At least 19 recordsLinked to original sources
PubMed1993

Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I.

A cDNA library prepared from the mouse osteoblastic cell line MC3T3-E1 was screened for the presence of specifically expressed genes by employing a combined subtraction hybridization/differential screening approach. A cDNA was identified and sequenced which encodes a protein designated osteoblast-specific factor 2 (OSF-2) comprising 811 amino acids. OSF-2 has a typical signal sequence, followed by a cysteine-rich domain, a fourfold repeated domain and a C-terminal domain. The protein lacks a typical transmembrane region. The fourfold repeated domain of OSF-2 shows homology with the insect protein fasciclin I. RNA analyses revealed that OSF-2 is expressed in bone and to a lesser extent in lung, but not in other tissues. Mouse OSF-2 cDNA was subsequently used as a probe to clone the human counterpart. Mouse and human OSF-2 show a high amino acid sequence conservation except for the signal sequence and two regions in the C-terminal domain in which 'in-frame' insertions or deletions are observed, implying alternative splicing events. On the basis of the amino acid sequence homology with fasciclin I, we suggest that OSF-2 functions as a homophilic adhesion molecule in bone formation.

3T3 Cells↗
PubMed1994

Insect proteins homologous to mammalian high mobility group proteins I/Y (HMG I/Y). Characterization and binding to linear and four-way junction DNA.

A chromosomal high mobility group (HMG) protein from an epithelial cell line of Chironomus tentans (Diptera) was purified to homogeneity and chemically characterized. cDNA clones encoding this protein were isolated and sequenced. The deduced amino acid sequence revealed a high similarity to HMG protein I of mammalia. This insect protein has therefore been designated cHMGI. It has a deduced molecular mass of 10,371 kDa and appears to be a product of a single gene copy. Similarly to mammalian HMGI/Y proteins the insect cHMGI protein has three putative DNA-binding motifs with a sequence K/RXRGRP that are each encoded by one exon of the gene. Using synthetic peptides we have shown that the first and the second motif are necessary for high-affinity binding of the protein to DNA. Protein cHMGI binds preferentially to AT-rich DNA with a half-saturation value of 1.1 nM. Both cHMGI and human HMGI proteins recognize specifically a four-way junction DNA. We have also purified a related protein with similar physico-chemical properties from Drosophila melanogaster Kc cells. The identification and characterization of HMGI proteins in insects with polytene chromosomes and with the cytologic and genetic potential of Chironomus and Drosophila opens new possibilities for studying function(s) of this group of chromosomal proteins.

Amino Acid Sequence↗
PubMed2005

ACE inhibitory activity in enzymatic hydrolysates of insect protein.

In this paper, ACE inhibitory activity in insect protein hydrolyzed by various enzymes (gastrointestinal proteases, alcalase, and thermolysin) is reported for the first time. Four insects of different insect orders were tested: Spodoptera littoralis (Lepidoptera), Bombyx mori (Lepidoptera), Schistocerca gregaria (Orthoptera), and Bombus terrestris (Hymenoptera). ACE inhibitory activity was measured by two different methods: a spectrophotometric method using FAPGG (2-furanacryloyl-phenylalanyl-glycyl-glycine) as substrate, and an HPLC method using dansyltriglycine (DTG) as substrate. Hydrolysis of the insect protein resulted in an increased ACE inhibitory activity. Overall, the highest ACE inhibitory activity was obtained after gastrointestinal digestion. These results suggest a role for insect protein as antihypertensive component in functional foods and nutraceuticals. Furthermore, the ACE inhibitory activity differed according to the method used. As a consequence, there is a need to standardize methodologies to evaluate ACE inhibitory activity.

Angiotensin-Converting Enzyme Inhibitors↗
PubMed1992

Insect proteins homologous to mammalian high mobility group protein 1. Characterization and DNA-binding properties.

Two chromosomal high mobility group (HMG) proteins from larvae of Chironomus thummi (Diptera) and from an epithelial cell line of Chironomus tentans were purified to homogeneity and chemically characterized. cDNA clones encoding these proteins were isolated from an expression library using an immunoscreening approach and were sequenced. The deduced amino acid sequences revealed their homology to HMG protein 1 of vertebrates. These insect proteins have therefore been designated cHMG1a and cHMG1b. They have a molecular mass of 12,915 and 12,019 kDa, respectively, and preferentially bind to AT-rich DNA. Indirect immunofluorescence microscopy with a polyclonal antibody showed the presence of cHMG1a and cHMG1b in condensed chromomeres but not in puffs, nucleoli, and cytoplasm. The cHMG1a and cHMG1b genes were both localized to a single band in region 14 of chromosome 1 of C. tentans and appear to be single copy genes. An immunologically related protein was purified from Drosophila melanogaster Kc cells. Its size and amino acid composition indicate that it is an HMG1 of D. melanogaster. On the other hand, our antibody did not recognize calf HMG1. The identification and characterization of HMG1 proteins in insects with polytene chromosomes opens new possibilities for studying function(s) of this group of chromosomal proteins.

Amino Acid Sequence↗
PubMed1999

A new class of hexahelical insect proteins revealed as putative carriers of small hydrophobic ligands.

BACKGROUND: THP12 is an abundant and extraordinarily hydrophilic hemolymph protein from the mealworm Tenebrio molitor and belongs to a group of small insect proteins with four highly conserved cysteine residues. Despite their sequence homology to odorant-binding proteins and pheromone-binding proteins, the function of these proteins is unclear. RESULTS: The first three-dimensional structure of THP12 has been determined by multidimensional NMR spectroscopy. The protein has a nonbundle helical structure consisting of six alpha helices. The arrangement of the alpha helices has a 'baseball glove' shape. In addition to the hydrophobic core, electrostatic interactions make contributions to the overall stability of the protein. NMR binding studies demonstrated the binding of small hydrophobic ligands to the single hydrophobic groove in THP12. Comparing the structure of THP12 with the predicted secondary structure of homologs reveals a common fold for this new class of insect proteins. A search with the program DALI revealed extensive similarity between the three-dimensional structure of THP12 and the N-terminal domain (residues 1-95) of recoverin, a member of the family of calcium-binding EF-hand proteins. CONCLUSIONS: Although the biological function of this new class of proteins is as yet undetermined, a general role as alpha-helical carrier proteins for small hydrophobic ligands, such as fatty acids or pheromones, is proposed on the basis of NMR-shift perturbation spectroscopy.

Amino Acid Sequence↗
PubMed2026

Gastrointestinal digestion governs insect protein hydrolysis and predicted bioactive peptide release: Species-dependent implications for functional food applications.

This study investigates the digestion of insect proteins and the release of predicted bioactive peptides during human gastrointestinal digestion. Using the Infogest in vitro model, mealworm, cricket, and black soldier fly larvae (BSFL) proteins were digested and analyzed through discovery proteomics and bioinformatics to identify predicted bioactive peptides. Sequential windowed acquisition of all theoretical fragment ion mass spectra (SWATH-MS) quantified insect proteins including predicted bioactive peptide precursor proteins, the precursors of predicted bioactive peptides. Results indicated that gastrointestinal digestion strongly influences peptide release, with the gastric phase exhibiting a richer predicted bioactive peptide profile than the small intestinal phase. Many predicted bioactive peptides were rapidly hydrolysed under small intestine conditions, which may lead to reduced stability or diminished activity in vivo, potentially explaining why certain peptides show strong bioactivity in vitro but limited effects in vivo. Additionally, predicted bioactive peptide release varied by insect species, influenced by genetic factors and peptide abundance. These findings highlight the importance of species selection and consideration of proteolytic digestion patterns in optimizing insect-derived bioactive peptides for functional foods and nutraceutical applications.

Animals↗
PubMed1992

Antibody to a 63 kilodalton insect protein in ankylosing spondylitis.

Ankylosing spondylitis (AS) is associated with antibodies to a heat shock puff on drosophila chromosomes. This observation was investigated by immunoblotting using extracts of the Schneider insect cell line and HeLa cells, before and after heat shock. An insect protein of 63 kilodaltons (but no equivalent human protein) was recognised by 21 (46%) of 46 serum samples from patients with AS, one of two patients with Reiter's syndrome, four (7%) of 60 patients with systemic lupus erythematosus, and two (4%) of 50 control subjects, but not by serum samples from patients with rheumatoid arthritis (RA). Previous heat shock did not appear to affect the strength of reaction, but ML-30, a monoclonal antibody to the mycobacterial 65 kilodalton heat shock protein (hsp65), also recognised an insect protein of 63 kilodaltons by immunoblotting. Antibodies to recombinant mycobacterial hsp65 were measured by enzyme linked immunosorbent assay (ELISA) in serum samples from patients with AS and RA. IgA binding to hsp65 was increased in 41% of AS and 19% of RA serum samples, but there was no correlation with detection of antibody to the insect 63 kilodalton protein.

Animals↗
PubMed1995

Proteins of crustacean exoskeleton: IV. Partial amino acid sequences of exoskeletal proteins from the Bermuda land crab, Gecarcinus lateralis, and comparisons to certain insect proteins.

As in all decapod Crustacea, the exoskeleton of the land crab Gecarcinus lateralis consists of four layers. Prior electrophoretic analysis of proteins extracted from these layers revealed an abundance of small M(r) proteins with acidic pIs are found in insect cuticle (O'Brien et al. [1991 Biol. Bull., 181:427-441). Further, immunological cross-reactivity between crab exoskeletal proteins and insect cuticular proteins has been demonstrated (Kumari and Skinner [1993] J. Exp. Zool., 265:195-210). Partial amino acid sequences of a number of proteins from the four exoskeletal layers are described here. Proteins were electrophoresed on two-dimensional (2D) gels, transferred to polyvinylidene difluoride (PVDF) membranes, and stained; individual spots were recovered and their N-termini were sequenced. In addition, a 14-kDa protein (pI = 5.4) from membranous layer (ML14) was eluted from 2D gels and digested with endoproteinase Lys-C; N-termini of its constituent peptides were sequenced. The two epicuticular proteins differed from each other. Three proteins with identical electrophoretic mobility isolated from exocuticle, endocuticle, and membranous layer appeared to have identical N termini, while another electrophoretically identical set from the three layers appeared identical with each other but differed in three positions from the first set. Two proteins from the membranous layer both had a mass of 25 kDa but different isoelectric points. Their sequences were indistinguishable from each other but clearly distinct from another membranous layer protein. Another distinct sequence was found in a 14-kDa protein from endocuticle, while a less acidic pair of 14-kDa proteins from endocuticle and membranous layer were quite similar to one another. The three internal peptide fragments from ML14 were distinct, but one had regions similar to the ML14 N terminus. One crab exoskeletal protein sequence was similar to some structural proteins of vertebrates, whereas others had motifs found in insect cuticular proteins. The sequence similarities identified did not account for the antibody cross-reactivity.

Amino Acid Sequence↗
PubMed2002

Highly-resolving two-dimensional electrophoresis for the study of insect proteins.

In this paper, we describe methods for isolation, purification and solubilization of insect proteins from various tissues, including lipid-rich fat body. An Australian locust, Oedaleus australis, and its associated dipteran parasite, Trichopsidea oestracea, provided the protein samples. Protein samples of locust fat body, haemolymph and body wall as well as parasite whole-body extracts were isolated and purified of lipids and salts using chloroform-methanol extraction. Proteins were solubilized using two types of enhanced solubilizing solutions and arrayed using two-dimensional electrophoresis. We demonstrated substantial differences between the body wall protein spectra of normal locusts and those parasitized by T. oestracea. Proteins more abundant in parasitized locusts include two 70 kDa proteins with an isoelectric point (pI) of about 5.5, one approximately 55 kDa protein cluster with a pI of about 4.7 and three 40 kDa proteins with pI values of around 5.6. Proteins that decreased in parasitized locusts include a group of 45 kDa proteins with pI values between 6 and 6.8, and a cluster of 22 to 23 kDa proteins with pI values of approximately 5.4 and 5.6.

Animals↗
PubMed1995

Molybdenum co-factor biosynthesis: the Arabidopsis thaliana cDNA cnx1 encodes a multifunctional two-domain protein homologous to a mammalian neuroprotein, the insect protein Cinnamon and three Escherichia coli proteins.

The molybdenum co-factor (Moco) is an essential part of all eukaryotic molybdoenzymes. It is a molybdopterin and reveals the same principal structure in eubacteria, archaebacteria and eukaryotes. This paper reports the isolation of cnx1, a cDNA clone of Arabidopsis thaliana which complements the Escherichia coli Moco mutant mogA. The mapping data of this cDNA correlate well with the mapping position of the A. thaliana molybdenum co-factor locus chl6. As mutants in chl6 are known to be repairable by high concentrations of molybdate, the defective gene is very likely to be involved in the last step of Moco biosynthesis, that is, the insertion of molybdenum into molybdopterin. The protein encoded by cnx1 shows a two-domain structure: the N-terminal domain is homologous to the E. coli Moco protein MoeA, the C-terminal domain is homologous to the E. coli Moco proteins MoaB and MogA, respectively. These homologies show that part of the prokaryotic Moco biosynthetic pathway accomplished by monofunctional proteins in E. coli, is performed by a single multifunctional protein in eukaryotes. In addition Cnx1 is homologous to the eukaryotic proteins Gephyrin, a rat neuroprotein, and Cinnamon, a Drosophila protein with a function in Moco biosynthesis. These proteins also show a two-domain structure but the order of the domains is inversed as compared with Cnx1. Southern analysis indicates the existence of at least one further member, in addition to the cnx1 gene, of this novel gene family in the Arabidopsis genome.

Amino Acid Sequence↗
PubMed1995

Insect cuticular proteins.

Insect cuticles are composite structural materials with mechanical properties optimal for their biological functions. The bulk properties of cuticles are to a large extent determined by the interactions between the various components, mainly the chitin filament system and the proteins. The various cuticular types show pronounced differences in mechanical properties, and it is suggested that these differences can be related to the properties of the individual proteins and to the degree of secondary stabilization (sclerotization). The amino acid sequences, which have been obtained for insect cuticular proteins either by direct sequencing of purified proteins or by deduction from corresponding DNA-sequences, are listed according to insect order and species. Extensive sequence similarity is observed among several cuticular proteins obtained from different insect orders. Other cuticular proteins are characterized by repeated occurrence of a few small motifs consisting mainly of hydrophobic residues. The latter group of proteins has so far only been reported from stiff cuticles. The possible relevance of the various motifs and repeats for protein interaction and the mechanical properties of cuticles is discussed.

Amino Acid Sequence↗
PubMed2005

The Photorhabdus Pir toxins are similar to a developmentally regulated insect protein but show no juvenile hormone esterase activity.

The genome of the insect pathogen Photorhabdus luminescens strain TT01 contains numerous genes predicting toxins and proteases. Within the P. luminescens TT01 genome, the products of two loci, plu 4093-plu 4092 and plu 4437-plu 4436, show oral insecticidal activity against both moth and mosquito larvae. The proteins encoded by these loci, here termed 'Photorhabdus insect related' (Pir) proteins A and B, show similarity both to delta-endotoxins from Bacillus thuringiensis (Bts) and a developmentally regulated protein from a beetle, Leptinotarsa decemlineata. The beetle protein has been inferred to possess juvenile hormone esterase (JHE) activity due to its developmentally regulated pattern of expression and the Photorhabdus proteins PirA and PirB have been proposed to be mimics of insect JHEs that can disrupt insect metamorphosis by metabolizing the insect growth regulator juvenile hormone (JH) [Nat. Biotechnol. 21 (2003) 1307-1313]. Here we confirm that, when injected together, PirA and PirB from two different Photorhabdus strains have insecticidal activity against caterpillars of the moth Galleria mellonella but show no oral activity against a second moth species Manduca sexta. Direct measurement of JHE activity, however, shows that the Pir proteins are not able to metabolise JH. These data show that the Pir proteins have no JHE activity, as suggested, but leave the mode of action of these interesting proteins uncertain.

Amino Acid Sequence↗
PubMed2000

A new secreted insect protein belonging to the immunoglobulin superfamily binds insulin and related peptides and inhibits their activities.

Insulin and related peptides are key hormones for the regulation of growth and metabolism. Here we describe a novel high affinity insulin-related peptide-binding protein (IBP) secreted from cells of the insect Spodoptera frugiperda. This IBP is composed of two Ig-like C2 domains, has a molecular mass of 27 kDa, binds human insulin with an affinity of 70 pm, and inhibits insulin signaling through the insulin receptor. The binding protein also binds insulin-like growth factors I and II, proinsulin, mini-proinsulin, and an insulin analog lacking the last 8 amino acids of the B-chain (des-octa peptide insulin) with high affinity, whereas an insulin analog with a Asp-B10 mutation bound with only 1% of the affinity of human insulin. This binding profile suggests that IBP recognizes a region that is highly conserved in the insulin superfamily but distinct from the classical insulin receptor binding site. The closest homologue of the Spodoptera frugiperda binding protein is the essential gene product IMP-L2, found in Drosophila, where it is implicated in neural and ectodermal development (Garbe, J. C., Yang, E., and Fristrom, J. W. (1993) Development 119, 1237-1250). Here we show that the IMP-L2 protein also binds insulin and related peptides, offering a possible functional explanation to the IMP-L2 null lethality.

Amino Acid Sequence↗
PubMed2002

Trichoplusia ni gloverin, an inducible immune gene encoding an antibacterial insect protein.

By using differential display PCR, we obtained a cDNA clone encoding a gloverin homologue from the cabbage looper, Trichoplusia ni. The expression of the gene was induced by bacterial infections. The gene codes for a 174 amino acid residue protein, including a signal sequence and a prosegment. The deduced mature protein is 14 kDa and shows 58% and 49% identity to P2 from Helicoverpa armigera and to Hyalophora gloveri gloverin, respectively. The protein was detected in hemolymph and hemocytes from bacteria-immunized animals. We expressed gloverin using the baculovirus expression system. N-terminal amino acid sequence analysis showed that the purified protein contained a propart. This progloverin inhibited the growth of E. coli and the activity is comparable to that of H. gloveri mature gloverin. Processing of progloverin was possible in vitro, using human furin.

Amino Acid Sequence↗
PubMed1992

Differential factor binding at the promoter of early baculovirus gene PE38 during viral infection: GATA motif is recognized by an insect protein.

Regulatory elements interacting with DNA-binding proteins have been investigated in the promoter sequence of the early PE38 gene in the Autographa californica nuclear polyhedrosis virus (AcNPV). A GATA motif located 50 nucleotides upstream of the PE38 transcriptional start site is recognized differentially in the course of infection. As demonstrated by footprint and gel mobility shift assays, the GATA sequences TTATCT are protected by nuclear extracts from uninfected Spodoptera frugiperda cells and from S. frugiperda cells early postinfection (p.i.) but not by S. frugiperda cell extracts isolated 40 h p.i. We have compared the binding capacity of the insect GATA-like protein with that of the vertebrate GATA-1 factor identified as erythroid-specific factor. Our results indicate that a factor present in mouse erythroleukemia cells, presumably GATA-1, can bind to the insect GATA motif and vice versa. Evidence from transient expression studies suggests that the mutated GATA sequences do not influence PE38 promoter activity in cell culture.

Animals↗
PubMed1990

[Identification and isolation of the protein insect toxin (alpha-latroinsectotoxin from venom of the spider Latrodectus mactans tredecimguttatus].

The crude venom of spider Latrodectus mactans tredecimguttatus was fractionated by the combination of anion exchange and hydrophobic chromatography. The biological activity of fraction was tested by means of: 1) estimation of toxicity for housefly larva; 2) intracellular recording of miniature excitatory potentials (MEPSPs) in blowfly larvae muscle fibres. As a result of sequential procedures of chromatography separation a homogeneous protein of 120 kilodalton molecular weight was obtained. This protein referred to alpha-latroinsectotoxin produced: 1) a great increase of the frequency of MEPSPs in the dose of 4.2.10(-10) M and its paralytic dose for fly larva was approximately 20 ng/species; 2) no influence of the MEPSPs after application in the dose of 1.2.10(-7) M to the neuromuscular junction of the frog.

Amino Acids↗
PubMed1985

Developmental expression of nuclear genes that encode mitochondrial proteins: insect cytochromes c.

To investigate tissue-specific developmental regulation of mitochondrial biogenesis, we studied the expression of the Manduca sexta (tobacco hornworm moth) thoracic muscle cytochrome c gene during adult eclosion and used this information to obtain a cDNA clone for this gene, which in turn was used to isolate the corresponding Drosophila melanogaster gene. Over the 3 days prior to adult Manduca emergence, mitochondrial inner membranes become progressively more electron dense and lamellar, and, while there is no accumulation of apocytochrome c, the amount of the holoprotein increases 40-fold per insect thorax. As determined by in vitro translation and blot hybridization analysis, the major thoracic muscle cytochrome c gene is primarily regulated at the transcriptional level, with cytochrome c mRNA increasing from less than 0.01% to 0.04% of total poly(A)+ RNA and declining to an undetectable level by day 2 after eclosion. Furthermore, the ratio of cytochrome c to the other cytochromes remains the same at all times, indicating that these components of the respiratory chain follow coordinated developmental programs. By using polysome immunoadsorption, a poly(A)+ RNA population of greater than or equal to 95% cytochrome c mRNA was isolated from thoracic muscle tissue and was used to construct a cDNA library, which was screened by hybrid selection/translation. We report the sequence of one of those clones, pMSc750, and its use to isolate the major thoracic muscle cytochrome c gene of Drosophila.

Animals↗