Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus

© 2020 Elsevier B.V. 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 che...

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Main Authors: Natapong Jupatanakul, Jutharat Pengon, Shiela Marie Gines Selisana, Waeowalee Choksawangkarn, Nongluck Jaito, Atiporn Saeung, Ratchanu Bunyong, Navaporn Posayapisit, Khrongkhwan Thammatinna, Nuttiya Kalpongnukul, Kittipat Aupalee, Trairak Pisitkun, Sumalee Kamchonwongpaisan
Format: Journal
Published: 2020
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http://cmuir.cmu.ac.th/jspui/handle/6653943832/69933
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Institution: Chiang Mai University
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spelling th-cmuir.6653943832-699332020-10-14T08:40:41Z Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus Natapong Jupatanakul Jutharat Pengon Shiela Marie Gines Selisana Waeowalee Choksawangkarn Nongluck Jaito Atiporn Saeung Ratchanu Bunyong Navaporn Posayapisit Khrongkhwan Thammatinna Nuttiya Kalpongnukul Kittipat Aupalee Trairak Pisitkun Sumalee Kamchonwongpaisan Agricultural and Biological Sciences Immunology and Microbiology Medicine © 2020 Elsevier B.V. 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°C but not 37°C. Two major protein bands of approximately 55 kDa and 110 kDa were present in spent medium cultured at 25°C but not at 37°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. 2020-10-14T08:22:17Z 2020-10-14T08:22:17Z 2020-12-01 Journal 18736254 0001706X 2-s2.0-85090405986 10.1016/j.actatropica.2020.105686 https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85090405986&origin=inward http://cmuir.cmu.ac.th/jspui/handle/6653943832/69933
institution Chiang Mai University
building Chiang Mai University Library
continent Asia
country Thailand
Thailand
content_provider Chiang Mai University Library
collection CMU Intellectual Repository
topic Agricultural and Biological Sciences
Immunology and Microbiology
Medicine
spellingShingle Agricultural and Biological Sciences
Immunology and Microbiology
Medicine
Natapong Jupatanakul
Jutharat Pengon
Shiela Marie Gines Selisana
Waeowalee Choksawangkarn
Nongluck Jaito
Atiporn Saeung
Ratchanu Bunyong
Navaporn Posayapisit
Khrongkhwan Thammatinna
Nuttiya Kalpongnukul
Kittipat Aupalee
Trairak Pisitkun
Sumalee Kamchonwongpaisan
Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
description © 2020 Elsevier B.V. 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°C but not 37°C. Two major protein bands of approximately 55 kDa and 110 kDa were present in spent medium cultured at 25°C but not at 37°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.
format Journal
author Natapong Jupatanakul
Jutharat Pengon
Shiela Marie Gines Selisana
Waeowalee Choksawangkarn
Nongluck Jaito
Atiporn Saeung
Ratchanu Bunyong
Navaporn Posayapisit
Khrongkhwan Thammatinna
Nuttiya Kalpongnukul
Kittipat Aupalee
Trairak Pisitkun
Sumalee Kamchonwongpaisan
author_facet Natapong Jupatanakul
Jutharat Pengon
Shiela Marie Gines Selisana
Waeowalee Choksawangkarn
Nongluck Jaito
Atiporn Saeung
Ratchanu Bunyong
Navaporn Posayapisit
Khrongkhwan Thammatinna
Nuttiya Kalpongnukul
Kittipat Aupalee
Trairak Pisitkun
Sumalee Kamchonwongpaisan
author_sort Natapong Jupatanakul
title Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
title_short Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
title_full Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
title_fullStr Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
title_full_unstemmed Serratia marcescens secretes proteases and chitinases with larvicidal activity against Anopheles dirus
title_sort serratia marcescens secretes proteases and chitinases with larvicidal activity against anopheles dirus
publishDate 2020
url https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85090405986&origin=inward
http://cmuir.cmu.ac.th/jspui/handle/6653943832/69933
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