Neutrophil ratio in the granulocyte infiltrate at the bite site could be associated with protection if cytotoxic cationic proteins released during eosinophil degranulation, or eosinophil-mediated phagocytosis, destroy the parasites before they use neutrophils as a Trojan horse to reach the intracellular compartment of deactivated macrophages. A major problem with this theoretical protection mechanism is that it needs to eliminate all parasites present in the infectious inoculum, otherwise an exacerbated form of the disease can be anticipated once surviving parasites infect deactivated macrophages. This is because their growth would proceed unhindered in the presence of the Th2-type cytokines that are necessary to promote the recruitment of eosinophils into tissues. From a vaccine development perspective this situation represents a conundrum: On the one hand, a Th2-driven vaccine targeting sand fly salivary proteins would be required to be 100% effective in eliminating the inoculated parasites at the sand fly bite site, and on the other hand, a Th1-driven vaccine targeting the same salivary proteins might mitigate the naturally acquired antisalivary immunity developed as a result of chronic exposure to sand fly saliva. The BluePort system might be an ideal tool to clarify this problem because their resident macrophages can be readily infected with Leishmania parasites. The identification of salivary molecules and epitopes capable of promoting the recruitment of eosinophils at the bite site is an important element of efforts to understand the molecular basis of pathogen transmission by hematophagous arthropods. One of the best characterized L. longipalpis salivary proteins has been shown to induce Th2-biased immune responses, but it is unknown whether it promotes dermal eosinophilia at the bite site. While it remains to be shown whether any of the glycans attached to L. longipalpis salivary proteins promotes dermal eosinophilia, it is intriguing that AAL, a lectin that recognizes L. longipalpis salivary glycoproteins, also recognize immunomodulatory glycans expressed in the eggshells of a pathogen, S. mansoni, that induces strong eosinophilic responses in the tissues of infected animals. The potential for structural similarity in glycans synthesized by arthropods and helminths illustrate the need to study the Dabrafenib Raf inhibitor evolution of the Golgi system in metazoans, and a comparative analysis of the repertoire of glycans that each species can synthesize. It has already been shown that structural similarity in fucosylated N-linked glycans synthesized by plants, insects and nematodes define one of the main cross-reactive epitopes recognized by antibodies of patients with allergies to foodstuff, pollen, insect bites and stings.