Functional expression of a peritrophin A-like SfPER protein is required for larval development in Spodoptera frugiperda (Lepidoptera: Noctuidae)

Peritrophins are associated with structural and functional integrity of peritrophic membranes (PM), structures composed of chitin and proteins. PM lines the insect midgut and has roles in digestion and protection from toxins. We report the full-length cDNA cloning, molecular characterization and fun...

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Bibliographic Details
Published in:	Scientific reports Vol. 9; no. 1; p. 2630
Main Authors:	Rodríguez-de la Noval, Claudia, Rodríguez-Cabrera, Lianet, Izquierdo, Laurent, Espinosa, Luis A., Hernandez, Daily, Ponce, Milagro, Moran-Bertot, Ivis, Tellez-Rodríguez, Pilar, Borras-Hidalgo, Orlando, Huang, Siliang, Kan, Yunchao, Wright, Denis J., Ayra-Pardo, Camilo
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 22-02-2019 Nature Publishing Group
Subjects:	38/22 38/77 38/89 38/90 631/337/505 631/45/612 82/1 82/16 82/29 82/58 82/80 82/83 Amino acid sequence Amino acids Biotechnology Chitin Cloning Eggs Enzymes Gene expression Genetic engineering Humanities and Social Sciences Insect control Insects Laboratories Larvae Larval development Midgut Mucin multidisciplinary Peptides Peritrophin Phylogenetics Phylogeny Proteins Science Science (multidisciplinary) Spodoptera frugiperda Structure-function relationships Toxins Western blotting
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Summary:	Peritrophins are associated with structural and functional integrity of peritrophic membranes (PM), structures composed of chitin and proteins. PM lines the insect midgut and has roles in digestion and protection from toxins. We report the full-length cDNA cloning, molecular characterization and functional analysis of SfPER, a novel PM peritrophin A protein, in Spodoptera frugiperda . The predicted amino acid sequence indicated SfPER’s domain structure as a CMCMC-type, consisting of a signal peptide and three chitin-binding (C) domains with two intervening mucin-like (M) domains. Phylogenetic analysis determined a close relationship between SfPER and another S. frugiperda PM peritrophin partial sequence. SfPER transcripts were found in larvae and adults but were absent from eggs and pupae. Chitin affinity studies with a recombinant SfPER-C1 peritrophin A-type domain fused to SUMO/His-tag confirmed that SfPER binds to chitin. Western blots of S. frugiperda larval proteins detected different sized variants of SfPER along the PM, with larger variants found towards the posterior PM. In vivo suppression of SfPER expression did not affect susceptibility of larvae to Bacillus thuringiensis toxin, but significantly decreased pupal weight and adult emergence, possibly due to PM structural alterations impairing digestion. Our results suggest SfPER could be a novel target for insect control.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	2045-2322 2045-2322
DOI:	10.1038/s41598-019-38734-0