Chitinase of Serratia marcescens and its toxicity to insects

Lysenko, О.

doi:10.1016/0022-2011(76)90101-4

Cited by 59 publications

(21 citation statements)

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“…Microbial chitinases have been used in mixing experiments to increase the potency of entomopathogenic microorganisms. Synergistic effects among chitinolytic enzymes and microbial insecticides have been known to occur since the early 1970s (Lysenko, 1976;Morris, 1976). Larvae of the spruce bud worm, Choristoneura fumiferana, died more rapidly when exposed to chitinase-Bt mixtures than when exposed to the enzyme or bacterium alone (Smirnoff et al, 1974).…”

Section: Discussionmentioning

confidence: 99%

Cloning and expression of chitinase A, B, and C (chiA, chiB, chiC) genes from Serratia marcescens originating from Helicoverpa armigera and determining their activities

Danismazoglu¹,

Demir²,

Sezen³

et al. 2015

Turk J Biol

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IntroductionChitin, a linear polymer of β-1,4-linked N-acetyl-Dglucosamine (GlcNAc), is one of the most abundant biopolymers in nature. It is the main component of the exoskeleton of many invertebrates such as crustaceans, insects, and spiders and a structural component of the cell walls of most fungi and algae. In insects it functions as scaffold material, supporting the cuticles of the epidermis and trachea as well as the peritrophic membrane (PM) lining the gut epithelium (Merzendorfer and Zimoch, 2003;Ruiz-Sanchez et al., 2005;Kuzu, 2008).Chitinases are glycosyl hydrolases that catalyze the hydrolytic degradation of chitin. Chitin, which is found in the structure of cuticles and peritrophic membranes, is degraded by the chitinase enzymes. The degradation decreases the feeding and defenses of the insect and weakens it. Therefore, chitinases are important enzymes that have potential for being used as biological control agents against harmful insects (Cohen, 1987;Debaditya et al., 2007;Kuzu, 2008). Chitinases have been detected in a great variety of organisms, including those that contain chitin, such as insects, crustaceans, yeasts, and fungi, and also organisms that do not contain chitin, such as bacteria, higher plants, and vertebrates. Several genera of bacteria, including Serratia (

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Section: Discussionmentioning

confidence: 99%

Cloning and expression of chitinase A, B, and C (chiA, chiB, chiC) genes from Serratia marcescens originating from Helicoverpa armigera and determining their activities

Danismazoglu¹,

Demir²,

Sezen³

et al. 2015

Turk J Biol

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“…At present, some 11 proteases have been described as being produced by several different strains of S. marcescens (e.g. Brenner, 1992), including chitinases (Lysenko, 1976). Poinar et al (1979) found that S. marcescens was capable of entering the hemocoel in tsetse flies, which died soon after from fatal septicemia.…”

Section: Discussionmentioning

confidence: 99%

Serratia marcescens as a bacterial pathogen of Rhagoletis pomonella flies (Diptera: Tephritidae)

Lauzon¹,

Bussert²,

Sjogren³

et al. 2003

Eur. J. Entomol.

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Abstract. A nonpigmenting strain of Serratia marcescens Bizio isolated from dead and apparently diseased wild apple maggot flies, Rhagoletis pomonella (Walsh), was shown to he pathogenic to healthy apple maggot flies upon ingestion. The microorganism was detected in live adult alimentary canal organs four days post ingestion hut produced death in some flies within 24 h when flies fed on a cell concentration of 4.7 x 104 cfu/ml and within 8 h when flies fed on filter-sterilized culture medium that previously contained a 21 h culture of S. marcescens. Increasing the cell concentration 10,000 fold did not lead to an increased rate of kill. Young flies (7-10 days old) were more susceptihle to infection leading to death than were older flies (21-28 days old). The potential use of S. marcescens cells as control agents against apple maggot flies is negated hy their pathogenicity to vertehrates; however, the potential use of toxic compounds produced hy this strain of S. marcescens is discussed.

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“…Similarly nematode chitinase (Fuhrman et al, 1992) that break down the protective sheath of the mosquito host, insect venoms that contain chitinase (Krishnan et al,1994), and bacterial chitinases have also been used. While bacterial chitinases, mixed with Bacillus thuringenesis enhanced the activity of microbial insecticides (Smirnoff 1974, Lysenko 1976, Sneh et al, 1983. Regev et al, (1996) reported enhanced toxicity towards Spodoptera littoralis after administration of low levels of truncated recombinant Bt toxin and a bacterial endochitinase at a concentration of 10µg/ml.…”

Section: Introductionmentioning

confidence: 99%

Expression of a Variant Chitinase Transcript of Helicoverpa armigera in E. coli

2016

IJSR

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Gene encoding for chitinase was isolated and sequenced from the cotton bollworm Helicoverpa armigera, using the polymerase chain reaction technique directed by primers designed from the chitinase cDNA of the same insect reported by Ahmad et al. (2003). The nucleotide sequence analysis suggested that the gene is of 1737 bp showing homolgy of 96% with the reference chitinase sequence (AY325496) and 80% homology with that of Manduca sexta, the first cloned insect chitinase gene (U02270). The cDNA encoded a polypeptide of 578 amino acids, short of 10 amino acid residues compared to reference sequence. The major differences in the protein sequence to the one reported earlier was in proline threonine linker region where four threonine residues were replaced by alanine and one threonine by serine and further, condensation of protein towards the C-terminal region. Surprisingly the protein sequence of chitin binding domain shows 98% homolgy to Lymantria dispar chitinase (KP337328.1) and 96% homology to Phyllonorycter ringoniella chitinase (JN607321.1) and 100% homology to the reference protein(AAQ91786.1). Expression of the gene in bacterial system resulted in the formation of inclusion bodies retaining enzymatic activity. Bioassay for insecticidal activity against Helicoverpa armigera showed 60% mortality for injection assay, reduction in larval weight gain in case of oral application and 40% mortality for topical application.

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Chitinase of Serratia marcescens and its toxicity to insects

Cited by 59 publications

References 0 publications

Cloning and expression of chitinase A, B, and C (chiA, chiB, chiC) genes from Serratia marcescens originating from Helicoverpa armigera and determining their activities

Cloning and expression of chitinase A, B, and C (chiA, chiB, chiC) genes from Serratia marcescens originating from Helicoverpa armigera and determining their activities

Serratia marcescens as a bacterial pathogen of Rhagoletis pomonella flies (Diptera: Tephritidae)

Expression of a Variant Chitinase Transcript of Helicoverpa armigera in E. coli

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