Inactivation of baculovirus by quinones formed in insect-damaged plant tissues

Gary Felton, Sean S. Duffey

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

The infectivity of the nuclear polyhedrosis virus, HzSNPV to Heliothis zea was significantly reduced when viral occlusion bodies were exposed to the plant phenolic chlorogenic acid in the presence of polyphenol oxidase. Chlorogenic acid is rapidly oxidized to the ortho-quinone, chlorogenoquinone, by foliar polyphenol oxidases of the tomato plant, Lycopersicon esculentum, when foliage is damaged during feeding by larval H. zea. Our results indicate that chlorogenoquinone, a powerful oxidizing agent, covalently binds to the occlusion bodies of HzSNPV and significantly reduces their digestibility and solubility under alkaline conditions. This binding is proposed to interfere with the infection process by impairing the release of infective virions in the midgut.

Original languageEnglish (US)
Pages (from-to)1221-1236
Number of pages16
JournalJournal of Chemical Ecology
Volume16
Issue number4
DOIs
StatePublished - Apr 1 1990

Fingerprint

Helicoverpa zea single nucleopolyhedrovirus
Catechol Oxidase
Chlorogenic Acid
Quinones
Helicoverpa zea
Baculoviridae
Lycopersicon esculentum
chlorogenic acid
quinones
catechol oxidase
Zea mays
Insects
plant tissues
inactivation
insect
Tissue
Nucleopolyhedrovirus
insects
infectivity
acid

All Science Journal Classification (ASJC) codes

  • Ecology, Evolution, Behavior and Systematics
  • Biochemistry

Cite this

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abstract = "The infectivity of the nuclear polyhedrosis virus, HzSNPV to Heliothis zea was significantly reduced when viral occlusion bodies were exposed to the plant phenolic chlorogenic acid in the presence of polyphenol oxidase. Chlorogenic acid is rapidly oxidized to the ortho-quinone, chlorogenoquinone, by foliar polyphenol oxidases of the tomato plant, Lycopersicon esculentum, when foliage is damaged during feeding by larval H. zea. Our results indicate that chlorogenoquinone, a powerful oxidizing agent, covalently binds to the occlusion bodies of HzSNPV and significantly reduces their digestibility and solubility under alkaline conditions. This binding is proposed to interfere with the infection process by impairing the release of infective virions in the midgut.",
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Inactivation of baculovirus by quinones formed in insect-damaged plant tissues. / Felton, Gary; Duffey, Sean S.

In: Journal of Chemical Ecology, Vol. 16, No. 4, 01.04.1990, p. 1221-1236.

Research output: Contribution to journalArticle

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