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Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
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Metadata
Document Title
Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
Description
Posayapisit N, Thammatinna K, Kalpongnukul N, Aupalee K, Pisitkun T, Kamchonwongpaisan S
Author
Jupatanakul N, Pengon J, Selisana SMG, Choksawangkarn W, Jaito N, Saeung A, Bunyong R, Posayapisit N, Thammatinna K, Kalpongnukul N, Aupalee K, Pisitkun T, Kamchonwongpaisan S
Name from Authors Collection
Scopus Author ID
56335715500
Scopus Author ID
56575640100
Scopus Author ID
56335715500
Affiliations
National Science & Technology Development Agency - Thailand; National Center Genetic Engineering & Biotechnology (BIOTEC); University of the Philippines System; University of the Philippines Los Banos; Burapha University; Chiang Mai University; Prince of Songkla University; Chulalongkorn University; Chulalongkorn University; Tokyo Institute of Technology
Type
Article
Source Title
ACTA TROPICA
Year
2020
Volume
212
Open Access
Green Submitted
Publisher
ELSEVIER
DOI
10.1016/j.actatropica.2020.105686
Format
Abstract
Vector control, the most efficient tool to reduce mosquito-borne disease transmission, has been compromised by the rise of insecticide resistance. Recent studies suggest the potential of mosquito-associated microbiota as a source for new biocontrol agents or new insecticidal chemotypes. In this study, we identified a strain of Serratia marcescens that has larvicidal activity against Anopheles dirus, an important malaria vector in Southeast Asia. This bacterium secretes heat-labile larvicidal macromolecules when cultured under static condition at 25 degrees C but not 37 degrees C. Two major protein bands of approximately 55 kDa and 110 kDa were present in spent medium cultured at 25 degrees C but not at 37 degrees C. The Liquid Chromatography-Mass Spectrometry (LC-MS) analyses of these two protein bands identified several proteases and chitinases that were previously reported for insecticidal properties against agricultural insect pests. The treatment with protease and chitinase inhibitors led to a reduction in larvicidal activity, confirming that these two groups of enzymes are responsible for the macromolecule's toxicity. Taken together, our results suggest a potential use of these enzymes in the development of larvicidal agents against Anopheles mosquitoes.
Keyword
Anopheles | Entomopathogen | Larvicidal | Mass spectrometry | Microbiota
Industrial Classification
Knowledge Taxonomy Level 1
Knowledge Taxonomy Level 2
Knowledge Taxonomy Level 3
Funding Sponsor
National Center for Genetic Engineering and Biotechnology [P1751134]
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Copyright
Rights
Publisher
Publication Source
WOS