Abstract
The female endoparasitoid wasps introduce venom accompanied by an egg into the larval hosts’ body cavity during oviposition. The venom contains a mixture of proteins that exploit the host’s biological processes, such as, regulating gene expression, disrupting immune signaling pathways, or inducing immune cell death to give a decided advantage to the incipient wasp to develop unchallenged. Drosophila possesses a highly conserved innate immune response that recognizes and neutralizes foreign microbes and macroparasites. The venom of Ganaspis hookeri (strain G1) endoparasitoid wasp has co-evolved to suppresses the humoral phase Drosophila’s innate immune response by inhibiting Ca2+ bursts needed to induce an immune response signaling pathway. The intracellular Ca2+ concentration of host plasmatocytes is altered via a venom specific homolog of the Sarco/endoplasmic reticulum calcium ATPase (SERCA) as a virulence factor. The venom SERCA (vSERCA) is able to significantly alter host intracellular Ca2+ homeostasis, disrupting cell signaling. SERCA is a multipass transmembrane protein, suggesting that vSERCA is likely packaged for transport through the venom into host plasmatocytes. Extracellular vesicles (EVs), or venosomes, to transport a variety of venom proteins and peptides. An excellent question is how vSERCA makes its way from the venom glands of G1 and into host plasmatocytes to affect Ca+2levels. Here I will explore how G1 uses venosomes to package vSERCA and other key virulence factors for transport from the venom gland, where they are produced, into host hemocytes. I characterize how G1 venom transports vSERCA and other important virulence factors necessary for regulating host signaling pathways essential for the Drosophila larval immune response, and the underlying biogenic mechanisms of venosome directed protein transport. These results are relevant to our understanding of the evolution of hymenopteran and related species.
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