Abstract
Peptidoglycan recognition proteins (PGRPs) are multifunctional pattern recognition proteins. Here, we report that a PGRP gene, BtPGRP, encodes a PGRP from the whitefly Bemisia tabaci (MEAM1) that binds and kills bacteria in vitro. We analyzed BtPGRP transcriptional profiling, and the distribution of the cognate protein within the midgut. Fungal infection and wasp parasitization induced expression of BtPGRP. Silencing BtPGRP with artificial media amended with dsRNA led to reduced expression of a gene encoding an antimicrobial peptide, B. tabaci c-type lysozyme. Begomovirus infection also led to increased expression of BtPGRP. We propose that BtPGRP has a potential Tomato yellow leaf curl virus (TYLCV) binding site because we detected in vitro interaction between BtPGRP and TYLCV by immunocapture PCR, and recorded the co-localization of TYLCV and BtPGRP in midguts. This work addresses a visible gap in understanding whitefly immunity and provides insight into how the whitefly immunity acts in complex mechanisms of Begomovirus transmission among plants.
Highlights
Peptidoglycan recognition proteins (PGRPs) are multifunctional pattern recognition proteins
By confirming the full length of BtPGRP sequence using both DNA and RNA of B. tabaci (MEAN1, MED and ZHJ1), we found that BtPGRP from the three cryptic species shared 99.9% identity
The data reported in this paper strongly support our hypothesis that a PGRP gene, BtPGRP, encodes a PGRP that binds and kills bacteria and that Begomovirus infection, except for Tobacco curly shoot virus (TbCSV), induces BtPGRP expression
Summary
Peptidoglycan recognition proteins (PGRPs) are multifunctional pattern recognition proteins. We report that a PGRP gene, BtPGRP, encodes a PGRP from the whitefly Bemisia tabaci (MEAM1) that binds and kills bacteria in vitro. Cellular and humoral defenses depend on surveillance by a microbial recognition system that includes pattern-recognition receptors capable of recognizing microbe-specific molecules, known as pathogen-associated molecular patterns[5]. In Drosophila, and probably most insects, some PGRPs, such as PGRP-SA, act in sensing and distinguishing categories of infecting microbes (Gram-positive; Gram-negative; fungal) and activating down-stream immune effector pathways, such as the immune deficiency www.nature.com/scientificreports/. These proteins, including PGRP-SC and PGRP-LB, act as negative modulators of the imd pathway, which protects flies from lethal excessive immune reaction to transient infection[12]. Two members of the heat-shock protein (HSP) family (HSP70 and BtHSP16) and a midgut protein (MGP) bind begomoviruses in vitro; HSP70 may act in protecting the vector against begomoviruses while translocating within the whitefly[22,23,24]
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