Analysis of bacteria-challenged wild silkmoth, Antheraea mylitta (lepidoptera) transcriptome reveals potential immune genes

Gandhe, Archana S.; Arunkumar, Kallare P.; John, Serene H.; Nagaraju, Javaregowda

doi:10.1186/1471-2164-7-184

Cited by 50 publications

(27 citation statements)

References 43 publications

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“…They include 3 lysozymes, 1 attacin, and 1 potential AMP with the high identity (67%) to M. sexta immune-induced protein-1 (IID-1)26. So far, little is known about IID except it was reported that it was highly immune induced 26 and putatively defensive against the pathogens 39. Based on the amino acid sequence similarities, these five transcripts were named as OfgLys5, Ofglys6, OfgLys10, OfgAtt, and OfgIID.…”

Section: Resultsmentioning

confidence: 99%

Identification and Expression Profile Analysis of Antimicrobial Peptide/Protein in Asian Corn Borer, Ostrinia furnacalis (Guenée)

Zhang¹,

Zhou²,

Cheng³

et al. 2013

Int. J. Biol. Sci.

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Antimicrobial peptides/proteins (AMPs) are a group of immune proteins that exhibit strong antibiotic properties against numerous infectious bacterial strains. They are evolutionarily conserved and present in every kingdom and phylum, ranging from prokaryotes to humans. We analyzed the transciptome from the larvae of Asian corn borer, Ostrinia furnacalis (Guenée), and identified several putative AMP transcripts, OfgLys5, OfgLys6, OfgLys10, OfgAtt, and OfgIID. OfgLys5, OfgLys6, and OfgLys10 are all highly homologous with c-type lysozymes, and OfgAtt shows significant identities with Lepidoptera attacin. The amino acid sequence of OfgLys5 and OfgLys6 possessed all conserved features critical for fundamental structure and function of c-type lysozyme, including the two catalytic sites, Glu32 and Asp50. OfgAtt is a typical glycine-rich protein. The antimicrobial activity of O. furnacalis hemolymph increased significantly after injection with Escherichia coli, Micrococcus luteus, or Beauveria bassiana. OfgAtt, IDD, and Lys6 are expressed at low level prior to the challenge, but strongly induced against Gram-positive and negative bacteria, and fungi. Under the same inducement conditions, the transcripts of these three genes elevated most when fifth instar larvae were injected. Therefore, O. furnacalis larvae are induced to produce antimicrobial materials in the hemolymph after the infection, and increase of lysozyme and attacin may contribute to the antimicrobial activity.

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Section: Resultsmentioning

confidence: 99%

Identification and Expression Profile Analysis of Antimicrobial Peptide/Protein in Asian Corn Borer, Ostrinia furnacalis (Guenée)

Zhang¹,

Zhou²,

Cheng³

et al. 2013

Int. J. Biol. Sci.

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“…So far, gloverins have been identified only in Lepidoptera , including H. armigera (Mackintosh et al, 1998a), T. ni (Lundstrom et al, 2002), G. mellonella (Seitz et al, 2003), Antheraea mylitta (Gandhe et al, 2006), M. sexta (Abdel-latief and Hilker, 2008; Xu et al, 2012), Diatraea saccharialis (Silva et al, 2010), Plutella xylostella (Etebari et al, 2011; Eum et al, 2007), S. exigua (Hwang and Kim, 2011), and B. mori (Kawaoka et al, 2008; Mrinal and Nagaraju, 2008). Gloverins are synthesized as pre-pro-proteins, and the N-terminal regions of pro-gloverins contain a conserved RXXR motif (Xu et al, 2012).…”

Section: Gloverinsmentioning

confidence: 99%

Insect antimicrobial peptides and their applications

Huiuk

Chowdhury

Huang

et al. 2014

Appl Microbiol Biotechnol

482

459

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Insects are one of the major sources of antimicrobial peptides/proteins (AMPs). Since observation of antimicrobial activity in the hemolymph of pupae from the giant silk moths Samia Cynthia and Hyalophora cecropia in 1974 and purification of first insect AMP (cecropin) from H. cecropia pupae in 1980, over 150 insect AMPs have been purified or identified. Most insect AMPs are small and cationic, and they show activities against bacteria and/or fungi, as well as some parasites and viruses. Insect AMPs can be classified into four families based on their structures or unique sequences: the α-helical peptides (cecropin and moricin), cysteine-rich peptides (insect defensin and drosomycin), proline-rich peptides (apidaecin, drosocin and lebocin), and glycine-rich peptides/proteins (attacin and gloverin). Among insect AMPs, defensins, cecropins, proline-rich peptides and attacins are common, while gloverins and moricins have been identified only in Lepidoptera. Most active AMPs are small peptides of 20–50 residues, which are generated from larger inactive precursor proteins or pro-proteins, but gloverins (~14 kDa) and attacins (~20 kDa) are large antimicrobial proteins. In this mini-review, we will discuss current knowledge and recent progress in several classes of insect AMPs, including insect defensins, cecropins, attacins, lebocins and other proline-rich peptides, gloverins, and moricins, with a focus on structural-functional relationships and their potential applications.

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“…Seroins were initially discovered in Galleria mellonella as part of silk producing machinery (Zurovec et al ., ). Seroins have not been assigned any specific function in silk production in spite of their occurrence in the silkgland, whereas their induced expression was noticed in the fat body of G. mellonella and in Antheraea mylitta upon injury and bacterial challenge respectively (Gandhe et al ., ; Korayem et al ., ). Seroins are secretory proteins which possess signal peptides different from structural components of silk (Nirmala et al ., ).…”

Section: Introductionmentioning

confidence: 98%

Characterization of antiviral and antibacterial activity ofBombyx moriseroin proteins

et al. 2014

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SummaryLepidopterans as other insects have a very potent innate immune system, which basically comprises cellular and humoral defence mechanisms against bacterial and fungal infections. In lepidopterans, not much is known about the defence mechanisms against viral pathogens, such as baculoviruses. Here we show that small silk proteins of the domesticated silkworm, Bombyx mori, called seroins, act as antiviral agents against a baculovirus pathogen, Bombyx mori nucleopolyhedrovirus (BmNPV). Involvement of these proteins in the inhibition of baculovirus infection was revealed by estimating the viral load upon their dsRNA-mediated knockdown. Additionally, we found through antimicrobial assays that seroins are potent inhibitors of bacterial growth. Binding competition assays followed by antimicrobial assays showed that seroins bind to peptidoglycan, a cell wall component of bacteria. Analysis of bacterial load upon knockdown of seroins resulted in higher proliferation of bacteria. Phylogenetic analysis showed the recent origin of seroins in a few moth species and duplication only in Bombycids. The antiviral and antibacterial activity of seroins shown in this study using several biochemical and molecular biological assays provide strong evidence to characterize them as antimicrobial proteins. Hence, we hypothesize that seroins are potent candidates for use in development of transgene-based disease resistant silkworm strains.

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Analysis of bacteria-challenged wild silkmoth, Antheraea mylitta (lepidoptera) transcriptome reveals potential immune genes

Cited by 50 publications

References 43 publications

Identification and Expression Profile Analysis of Antimicrobial Peptide/Protein in Asian Corn Borer, Ostrinia furnacalis (Guenée)

Identification and Expression Profile Analysis of Antimicrobial Peptide/Protein in Asian Corn Borer, Ostrinia furnacalis (Guenée)

Insect antimicrobial peptides and their applications

Characterization of antiviral and antibacterial activity ofBombyx moriseroin proteins

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