title: Implication of Bemisia tabaci heat shock protein 70 in Begomovirus-whitefly interactions.
abstract: The whitefly Bemisia tabaci (Gennadius) is a major cosmopolitan pest capable of feeding on hundreds of plant species and transmits several major plant viruses. The most important and widespread viruses vectored by B. tabaci are in the genus Begomovirus, an unusual group of plant viruses owing to their small, single-stranded DNA genome and geminate particle morphology. B. tabaci transmits begomoviruses in a persistent circulative nonpropagative manner. Evidence suggests that the whitefly vector encounters deleterious effects following Tomato yellow leaf curl virus (TYLCV) ingestion and retention. However, little is known about the molecular and cellular basis underlying these coevolved begomovirus-whitefly interactions. To elucidate these interactions, we undertook a study using B. tabaci microarrays to specifically describe the responses of the transcriptomes of whole insects and dissected midguts following TYLCV acquisition and retention. Microarray, real-time PCR, and Western blot analyses indicated that B. tabaci heat shock protein 70 (HSP70) specifically responded to the presence of the monopartite TYLCV and the bipartite Squash leaf curl virus. Immunocapture PCR, protein coimmunoprecipitation, and virus overlay protein binding assays showed in vitro interaction between TYLCV and HSP70. Fluorescence in situ hybridization and immunolocalization showed colocalization of TYLCV and the bipartite Watermelon chlorotic stunt virus virions and HSP70 within midgut epithelial cells. Finally, membrane feeding of whiteflies with anti-HSP70 antibodies and TYLCV virions showed an increase in TYLCV transmission, suggesting an inhibitory role for HSP70 in virus transmission, a role that might be related to protection against begomoviruses while translocating in the whitefly.
authors.affiliation: Leibniz Institute DSMZ-German Collection of Microorganisms and Cell Cultures, Plant Virus Department, Braunschweig, Germany.
authors.forename: Monika
authors.initials: M
authors.lastname: Götz
authors.forename: Smadar
authors.initials: S
authors.lastname: Popovski
authors.forename: Mario
authors.initials: M
authors.lastname: Kollenberg
authors.forename: Rena
authors.initials: R
authors.lastname: Gorovits
authors.forename: Judith K
authors.initials: JK
authors.lastname: Brown
authors.forename: Joseph M
authors.initials: JM
authors.lastname: Cicero
authors.forename: Henryk
authors.initials: H
authors.lastname: Czosnek
authors.forename: Stephan
authors.initials: S
authors.lastname: Winter
authors.forename: Murad
authors.initials: M
authors.lastname: Ghanim
mesh_terms: D000818:Animals; D001483:Base Sequence; D053839:Begomovirus / Q000502:physiology*; D015153:Blotting, Western; D017931:DNA Primers; D004591:Electrophoresis, Polyacrylamide Gel; D020224:Expressed Sequence Tags; D018840:HSP70 Heat-Shock Proteins / Q000235:genetics / Q000502:physiology*; D006430:Hemiptera / Q000378:metabolism / Q000502:physiology* / Q000821:virology; D020411:Oligonucleotide Array Sequence Analysis; D060888:Real-Time Polymerase Chain Reaction
chemical_list: D017931:DNA Primers; D018840:HSP70 Heat-Shock Proteins