Novel insecticidal chitinase from the insect pathogen Xenorhabdus nematophila

Mahmood, Saquib; Kumar, Mrityunjay; Kumari, Punam; Mahapatro, G. K.; Banerjee, Nirupama; Sarin, Neera Bhalla

doi:10.1016/j.ijbiomac.2020.05.078

Cited by 20 publications

(18 citation statements)

References 81 publications

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“…This confirmed that CpCHI4 could be a potent candidate gene to tackle H. armigera damage on crops corroborating with the demonstration of utilization of chitinase genes from various sources to control lepidopteron pests 13,48 . Furthermore, such genes of biochemical relevance to both insects as well as plants can be useful for resistance management, which otherwise has been a concern.…”

Section: Resultssupporting

confidence: 72%

Characterization and in planta validation of a CHI4 chitinase from Cajanus platycarpus (Benth.) Maesen for its efficacy against pod borer, Helicoverpa armigera (Hübner)

Rathinam

Marimuthu

Tyagi

et al. 2021

Pest Management Science

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BACKGROUND Pigeonpea, Cajanus cajan is one of the economically important legume food crops and a major source of dietary proteins. Management of pod borer, Helicoverpa armigera has been prominent among crop improvement programs. Lack of resistance sources in the cultivated germplasm and crossing incompatibility with pod borer‐resistant wild relatives have prompted biotechnological interventions. Identification and exploitation of genes from pigeonpea wild relatives in host plant resistance towards the pod borer assumes pertinence. Dynamic transcriptome analysis of the wild relative vis a vis cultivated pigeonpea identified a CHI4 chitinase as one of the putative insect resistance genes. RESULTS The study presents variations in important amino acids in CHI4 chitinases from C. cajan and its wild relative C. platycarpus. Comparative protein modeling and docking analysis of the two proteins demonstrated differences in substrate binding efficacy of the chitinase from C. platycarpus which resulted in a minimum binding energy of −8.7 kcal mol−1. Furthermore, we successfully evaluated the insecticidal activity of the chitinase from C. platycarpus against H. armigera challenge through heterologous expression in tobacco. Molecular characterization of transgenic plants confirmed that their efficacy against H. armigera was a result of the integration of CHI4 from C. platycarpus. CONCLUSION Docking analysis demonstrated effective substrate interaction as a possible reason for efficacy against pod borer in the chitinase from C. platycarpus. This was authenticated by successful overexpression and bioefficacy assessment against H. armigera in tobacco. The CHI4 gene from C. platycarpus can be useful in the mitigation of H. armegira in pigeonpea as well as in other crops. © 2021 Society of Chemical Industry

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Section: Resultssupporting

confidence: 72%

Characterization and in planta validation of a CHI4 chitinase from Cajanus platycarpus (Benth.) Maesen for its efficacy against pod borer, Helicoverpa armigera (Hübner)

Rathinam

Marimuthu

Tyagi

et al. 2021

Pest Management Science

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“…A successful symbiotic complex needs to be able to kill the available insect prey more efficiently than other alternatives. For this, the EPB should produce toxins [ 87 , 88 , 89 , 90 , 91 ].…”

Section: Coevolution and Co-speciation Of Epn/epb Symbiotic Associationsmentioning

confidence: 99%

Type Strains of Entomopathogenic Nematode-Symbiotic Bacterium Species, Xenorhabdus szentirmaii (EMC) and X. budapestensis (EMA), Are Exceptional Sources of Non-Ribosomal Templated, Large-Target-Spectral, Thermotolerant-Antimicrobial Peptides (by Both), and Iodinin (by EMC)

Fodor

Gualtieri²,

Zeller

et al. 2022

Pathogens

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Antimicrobial multidrug resistance (MDR) is a global challenge, not only for public health, but also for sustainable agriculture. Antibiotics used in humans should be ruled out for use in veterinary or agricultural settings. Applying antimicrobial peptide (AMP) molecules, produced by soil-born organisms for protecting (soil-born) plants, seems a preferable alternative. The natural role of peptide-antimicrobials, produced by the prokaryotic partner of entomopathogenic-nematode/bacterium (EPN/EPB) symbiotic associations, is to sustain monoxenic conditions for the EPB in the gut of the semi-anabiotic infective dauer juvenile (IJ) EPN. They keep pathobiome conditions balanced for the EPN/EPB complex in polyxenic (soil, vanquished insect cadaver) niches. Xenorhabdus szentirmaii DSM16338(T) (EMC), and X. budapestensis DSM16342(T) (EMA), are the respective natural symbionts of EPN species Steinernema rarum and S. bicornutum. We identified and characterized both of these 15 years ago. The functional annotation of the draft genome of EMC revealed 71 genes encoding non-ribosomal peptide synthases, and polyketide synthases. The large spatial Xenorhabdus AMP (fabclavine), was discovered in EMA, and its biosynthetic pathway in EMC. The AMPs produced by EMA and EMC are promising candidates for controlling MDR prokaryotic and eukaryotic pathogens (bacteria, oomycetes, fungi, protozoa). EMC releases large quantity of iodinin (1,6-dihydroxyphenazine 5,10-dioxide) in a water-soluble form into the media, where it condenses to form spectacular water-insoluble, macroscopic crystals. This review evaluates the scientific impact of international research on EMA and EMC.

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“…This heterologous recombinant chitinase showed biocontrol activity against the larvae of H. armigera . The LD 50 value was 20 µg/g, which caused 51.5% larval mortality on day 3 [ 47 ]. Further, chitinase production is also induced by the attack of phytopathogens in plant seeds, stems, tuber, and flowers.…”

Section: Microbial Fermentation For Chitinase Productionmentioning

confidence: 99%

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

Poria

Rana

Kumari

et al. 2021

Biology

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Chitinases are a large and diversified category of enzymes that break down chitin, the world’s second most prevalent polymer after cellulose. GH18 is the most studied family of chitinases, even though chitinolytic enzymes come from a variety of glycosyl hydrolase (GH) families. Most of the distinct GH families, as well as the unique structural and catalytic features of various chitinolytic enzymes, have been thoroughly explored to demonstrate their use in the development of tailor-made chitinases by protein engineering. Although chitin-degrading enzymes may be found in plants and other organisms, such as arthropods, mollusks, protozoans, and nematodes, microbial chitinases are a promising and sustainable option for industrial production. Despite this, the inducible nature, low titer, high production expenses, and susceptibility to severe environments are barriers to upscaling microbial chitinase production. The goal of this study is to address all of the elements that influence microbial fermentation for chitinase production, as well as the purifying procedures for attaining high-quality yield and purity.

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Novel insecticidal chitinase from the insect pathogen Xenorhabdus nematophila

Cited by 20 publications

References 81 publications

Characterization and in planta validation of a CHI4 chitinase from Cajanus platycarpus (Benth.) Maesen for its efficacy against pod borer, Helicoverpa armigera (Hübner)

Characterization and in planta validation of a CHI4 chitinase from Cajanus platycarpus (Benth.) Maesen for its efficacy against pod borer, Helicoverpa armigera (Hübner)

Type Strains of Entomopathogenic Nematode-Symbiotic Bacterium Species, Xenorhabdus szentirmaii (EMC) and X. budapestensis (EMA), Are Exceptional Sources of Non-Ribosomal Templated, Large-Target-Spectral, Thermotolerant-Antimicrobial Peptides (by Both), and Iodinin (by EMC)

Current Perspectives on Chitinolytic Enzymes and Their Agro-Industrial Applications

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