Hemolin is an immunoglobulin-like protein exclusively found in Lepidoptera (moths and butterflies). It was first discovered in immune-challenged pupae of Hyalophora cecropia [1] and Manduca sexta . [2]
Hemolin has a horseshoe crystal structure [3] with four domains and resembles the developmental protein neuroglian.
Hemolin increases 18-fold up to 7 mg/ml following injection of bacteria in H. cecropia. Induction of Hemolin in moths after bacterial injection have been shown in several species including Antheraea pernyi , [4] Bombyx mori , Helicoverpa zea , [5] Heliothis virescens , [6] Hyphantria cunea , [7] and Samia cynthia . [8]
Hemolin has also been suggested to participate in the immune response to virus infection [9] and shown to bind to virus particles. [10] It is expressed in response to dsRNA in a dose-dependent manner. [11] Galleria melonella responds to caffeine intake by increased Hemolin protein expression. [12]
Hemolin is thought to be a gene duplication of the developmental protein neuroglian, [13] but has lost two of the protein domains that neuroglian contains. In the potential function as a developmental protein, Hemolin has been shown to increase close to pupation in Manduca sexta , [14] and is induced during diapause and by 20-Hydroxyecdysone in Lymantria dispar . [15] RNAi of Hemolin causes malformation in H. cecropia. [16]
Juvenile hormones (JHs) are a group of acyclic sesquiterpenoids that regulate many aspects of insect physiology. The first discovery of a JH was by Vincent Wigglesworth. JHs regulate development, reproduction, diapause, and polyphenisms.The chemical formula for juvenile hormone is .
In animal dormancy, diapause is the delay in development in response to regular and recurring periods of adverse environmental conditions. It is a physiological state with very specific initiating and inhibiting conditions. The mechanism is a means of surviving predictable, unfavorable environmental conditions, such as temperature extremes, drought, or reduced food availability. Diapause is observed in all the life stages of arthropods, especially insects.
Defensins are small cysteine-rich cationic proteins across cellular life, including vertebrate and invertebrate animals, plants, and fungi. They are host defense peptides, with members displaying either direct antimicrobial activity, immune signalling activities, or both. They are variously active against bacteria, fungi and many enveloped and nonenveloped viruses. They are typically 18-45 amino acids in length, with three or four highly conserved disulphide bonds.
Leucyl aminopeptidases are enzymes that preferentially catalyze the hydrolysis of leucine residues at the N-terminus of peptides and proteins. Other N-terminal residues can also be cleaved, however. LAPs have been found across superkingdoms. Identified LAPs include human LAP, bovine lens LAP, porcine LAP, Escherichia coli LAP, and the solanaceous-specific acidic LAP (LAP-A) in tomato.
Cotesia congregata is a parasitoid wasp of the genus Cotesia. The genus is particularly noted for its use of polydnaviruses. Parasitoids are distinct from true parasites in that a parasitoid will ultimately kill its host or otherwise sterilize it.
Chemosensory proteins (CSPs) are small soluble proteins which mediate olfactory recognition at the periphery of sensory receptors in insects, similarly to odorant-binding proteins. The typical structure of CSPs is made of six or seven α-helical chains of about 110-120 amino acids, including four cysteines that build two small loops, two adjacent disulfide bridges, and a globular "prism-like" functional structure [5]. Three CSP structures have been solved in moths and locusts [5-8].
The enzyme juvenile hormone esterase (EC 3.1.1.59, systematic name methyl-(2E,6E,10R)-10,11-epoxy-3,7,11-trimethyltrideca-2,6-dienoate acylhydrolase, JH esterase) catalyzes the hydrolysis of juvenile hormone:
Cecropins are antimicrobial peptides. They were first isolated from the hemolymph of Hyalophora cecropia, whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.
Antheraea pernyi, the Chinese (oak) tussar moth, Chinese tasar moth or temperate tussar moth, is a large moth in the family Saturniidae. The species was first described by Félix Édouard Guérin-Méneville in 1855. Antheraea roylei is an extremely close relative, and the present species might actually have evolved from ancestral A. roylei by chromosome rearrangement.
Juvenile hormone epoxide hydrolase (JHEH) is an enzyme that inactivates insect juvenile hormones. This inactivation is accomplished through hydrolysis of the epoxide functional group contained within these hormones into diols. JHEH is one of two enzymes involved in the termination of signaling properties of the various juvenile hormones. The other is juvenile-hormone esterase, or JHE.
Attacin is a glycine-rich protein of about 20 kDa belonging to the group of antimicrobial peptides (AMP). It is active against Gram-negative bacteria.
Peptidoglycan recognition proteins (PGRPs) are a group of highly conserved pattern recognition receptors with at least one peptidoglycan recognition domain capable of recognizing the peptidoglycan component of the cell wall of bacteria. They are present in insects, mollusks, echinoderms and chordates. The mechanism of action of PGRPs varies between taxa. In insects, PGRPs kill bacteria indirectly by activating one of four unique effector pathways: prophenoloxidase cascade, Toll pathway, IMD pathway, and induction of phagocytosis. In mammals, PGRPs either kill bacteria directly by interacting with their cell wall or outer membrane, or hydrolyze peptidoglycan. They also modulate inflammation and microbiome and interact with host receptors.
Intelectins are lectins expressed in humans and other chordates. Humans express two types of intelectins encoded by ITLN1 and ITLN2 genes respectively. Several intelectins bind microbe-specific carbohydrate residues. Therefore, intelectins have been proposed to function as immune lectins. Even though intelectins contain fibrinogen-like domain found in the ficolins family of immune lectins, there is significant structural divergence. Thus, intelectins may not function through the same lectin-complement pathway. Most intelectins are still poorly characterized and they may have diverse biological roles. Human intelectin-1 (hIntL-1) has also been shown to bind lactoferrin, but the functional consequence has yet to be elucidated. Additionally, hIntL-1 is a major component of asthmatic mucus and may be involved in insulin physiology as well.
Drosomycin is an antifungal peptide from Drosophila melanogaster and was the first antifungal peptide isolated from insects. Drosomycin is induced by infection by the Toll signalling pathway, while expression in surface epithelia like the respiratory tract is instead controlled by the immune deficiency pathway (Imd). This means that drosomycin, alongside other antimicrobial peptides (AMPs) such as cecropins, diptericin, drosocin, metchnikowin and attacin, serves as a first line defence upon septic injury. However drosomycin is also expressed constitutively to a lesser extent in different tissues and throughout development.
Hans Gustaf Boman (1924-2008) was a Swedish microbiologist with a special focus on innate immunity. Boman was born on 16 August 1924 in Engelbrekt Parish, Stockholm, Sweden, and died on 3 December 2008. Boman's pioneering research on insect immunity formed the basis for the Nobel Prize in Physiology or Medicine 2011.
James "Jim" William Truman is an American chronobiologist known for his seminal research on circadian rhythms in silkmoth (Saturniidae) eclosion, particularly the restoration of rhythm and phase following brain transplantation. He is a professor emeritus at the University of Washington and a former senior fellow at Howard Hughes Medical Institution Janelia Research Campus.
Phenoloxidase system is a major defense system in many invertebrates which ultimately leads to melanization of pathogens and damaged tissues. The process of melanization depends on activation of the enzyme phenoloxidase (PO) which is controlled by the prophenoloxidase (proPO) activation system.
Nancy Elizabeth Beckage was an American entomologist known for her work on host–parasitoid interactions. She held professorships in entomology and in cell biology and neuroscience at the University of California, Riverside.
Michael R. Kanost is a University Distinguished Professor in the Department of Biochemistry and Molecular Biophysics at Kansas State University.
Cytochrome P450, family 9, also known as CYP9, is a cytochrome P450 family found in Insect genome, CYP9 and insect CYP6 family belong to the same clan as mammalian CYP3 and CYP5 families. The first gene identified in this family is the CYP9A1 from the Heliothis virescens, which is involved in thiodicarb insecticide resistance. Subfamily CYP9A in Lepidopteran play important roles in insecticide resistance, can metabolize esfenvalerate efficiently.