Spatial and temporal synthesis of Mamestra configurata peritrophic matrix through a larval stadium

TOPRAK U., Hegedus D. D., Baldwin D., Coutu C., Erlandson M.

INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol.54, pp.89-97, 2014 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 54
  • Publication Date: 2014
  • Doi Number: 10.1016/j.ibmb.2014.09.002
  • Journal Name: INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.89-97
  • Keywords: Peritrophic matrix formation, Peritrophin, Insect intestinal mucin, Chitin synthase, Chitin deacetylase, Chitinase, N-acetylglucosaminidase, Mamestra configurata, CHITIN SYNTHASE GENES, MANDUCA-SEXTA, MEMBRANE-STRUCTURE, SPODOPTERA-FRUGIPERDA, TRICHOPLUSIA-NI, BERTHA ARMYWORM, LUCILIA-CUPRINA, BOMBYX-MORI, PROTEIN, MIDGUT
  • Ankara University Affiliated: Yes

Abstract

The structure and synthesis of the Mamestra configurata peritrophic matrix (PM) was examined at various time points during a larval stadium. Bright field and confocal fluorescence microscopy revealed major differences between the PM of feeding and molting larvae. The PM from feeding larvae was thinner and composed of approximately 5-10 layers. In contrast, mid-molt larvae had a chitinaceaous PM composed of multiple thick layers which filled most of the midgut lumen. PM synthesis initiates in the anterior midgut, based on the expression of genes encoding chitin synthase-2 (CHS-2), coincident with the incorporation of the major structural PM proteins (McIIM1, McIIM2 and McPM1). This is followed by reinforcement with other PM proteins (McIIM3 and McIIM4) as it moves toward the posterior of the midgut.