Comparison of the potential activities of viral and bacterial chitinases
Background Chitin, a long-chain polymer of N -acetylglucosamine, is a major structural component of the insect exoskeleton and the peritrophic membrane (PM). Chitinases are able to effectively break down glycosidic bonds of chitin polymer thus can be used in agriculture to control plant pathogen ins...
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| Published in: | Egyptian journal of biological pest control Vol. 31; no. 1; pp. 1 - 7 |
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| Main Authors: | , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
Berlin/Heidelberg
Springer Berlin Heidelberg
12-06-2021
Springer Nature B.V SpringerOpen |
| Subjects: | |
| Online Access: | Get full text |
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| Summary: | Background
Chitin, a long-chain polymer of
N
-acetylglucosamine, is a major structural component of the insect exoskeleton and the peritrophic membrane (PM). Chitinases are able to effectively break down glycosidic bonds of chitin polymer thus can be used in agriculture to control plant pathogen insects. These enzymes can be synthesized by higher plants, animals, protista, bacteria, and viruses.
Results
In this study, viral and bacterial chitinases were compared for their potential activity on a laboratory test insect. The genes encoding chitinases of
Autographa californica nucleopolyhedrovirus
(AcNPV) and
Cydia pomonella granulovirus
(CpGV) were amplified from genomic DNAs by PCR and cloned into the pET-28a (+) expression vector. The chitinase proteins of these 2 viruses (AcNPV-Chi, CpGV-Chi) and
Serratia marcescens
chitinase C (ChiC) protein which was previously cloned were overexpressed in
Escherichia coli
. Expressed proteins were purified and confirmed by western blot analysis as 50, 63, and 68 kDa for AcNPV, CpGV, and
S. marcescens
chitinases, respectively. Enzyme activities of the chitinases were confirmed. Chitinases were also compared to each other in silico. The insecticidal effects of these proteins were evaluated on
Galleria mellonella
L. larvae. Bioassays were performed on the 3rd instar larvae for each chitinase protein in triplicate. The results showed that although there were differences in enzymatic activities and domain organizations, all 3 microbial chitinases produced almost the same level of insecticidal activity on the test insect. LC
50
and LT
50
values were compatible with the mortality results. These results were a preanalysis for comparing the effects of microbial chitinases.
Conclusion
Potential activity experiments should be carried out on more insects to provide detailed information on the insecticidal effects of bacterial and viral chitinases. |
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| ISSN: | 2536-9342 1110-1768 2536-9342 |
| DOI: | 10.1186/s41938-021-00435-0 |