Comparative study of gene expression and major proteins' function of laticifers in lignified and unlignified organs of mulberry.

A laticifer is a cell involved in plant defense against biotic stresses such as herbivores and microorganisms; however, its gene expression is poorly understood. We compared protein accumulation and transcriptomes among laticifers of lignified and unlignified organs of mulberry (Morus alba), which has a non-articulated, branched type of laticifer. LA-a (equivalent to MLX56) and its homolog LA-b (insecticidal chitinase-like proteins containing two chitin-binding domains) were major proteins in laticifers of unlignified organs, and another protein (LA-c) was a major protein in laticifers of lignified organs. Purification, cDNA cloning, and bioassay of LA-c revealed that LA-c was an acidic class I chitinase having antifungal but not insecticidal activity. Comparative mRNA-Seq analysis using a GS-FLX revealed transcripts of other possible defense-related proteins. Jacalin-like lectin, galacturonase-inhibitor, and pathogenesis-related proteins were also abundant; however, the relative amounts differed among laticifers of lignified and unlignified organs. The results suggest a discontinuous laticifer network in planta and adaptation to different potential enemies among these organs.

Two chitinase-like proteins abundantly accumulated in latex of mulberry show insecticidal activity.

BACKGROUND: Plant latex is the cytoplasm of highly specialized cells known as laticifers, and is thought to have a critical role in defense against herbivorous insects. Proteins abundantly accumulated in latex might therefore be involved in the defense system. RESULTS: We purified latex abundant protein a and b (LA-a and LA-b) from mulberry (Morus sp.) and analyzed their properties. LA-a and LA-b have molecular masses of approximately 50 and 46 kDa, respectively, and are abundant in the soluble fraction of latex. Western blotting analysis suggested that they share sequence similarity with each other. The sequences of LA-a and LA-b, as determined by Edman degradation, showed chitin-binding domains of plant chitinases at the N termini. These proteins showed small but significant chitinase and chitosanase activities. Lectin RCA120 indicated that, unlike common plant chitinases, LA-a and LA-b are glycosylated. LA-a and LA-b showed insecticidal activities when fed to larvae of the model insect Drosophila melanogaster. CONCLUSIONS: Our results suggest that the two LA proteins have a crucial role in defense against herbivorous insects, possibly by hydrolyzing their chitin.