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In photovoltaic (PV) panels consisting of multiple substrings connected in series, mismatch in substring characteristics due to partial shading causes the significant reduction in energy yield and the occurrence of multiple maximum power points. In solar roofs of plug-in hybrid electric vehicles (PHEVs), substring characteristics are always unavoidably mismatched due to the curvature of solar roofs, resulting in the mismatch issues similar to partial shading. Various kinds of differential power processing (DPP) converters have been proposed to preclude mismatch issues in traditional flat PV panels. The key contributions and novelties of this paper are summarized as follows. Firstly, uneven irradiance on the solar roof of Prius PHEVs is investigated. Secondly, existing DPP converter architectures are reviewed to select a proper DPP converter topology for PHEV applications. Thirdly, the selected topology is improved to be better suitable for PHEV applications, followed by the detailed operation analysis. Lastly, the experimental results of the laboratory and field testing using a prototype are presented. Field testing using an actual solar roof of Prius PHEV was performed, and the results demonstrated the daily energy yield enhancement of 4%–5% by the proposed DPP converter.

Summary Various C-type lectin receptors (CLRs), including Mincle and Dectin-2, function as pattern recognition receptors and play a central role in immunity to fungal pathogens. However, the precise structures of the CLR ligands in various pathogenic fungi have yet to be completely defined. Here we report that Malassezia , an opportunistic skin fungal pathogen, is cooperatively recognized by Mincle and Dectin-2 through distinct ligands. Solvent-based fractionation revealed that Mincle and Dectin-2 recognize lipophilic and hydrophilic components of Malassezia , respectively. Mass spectrometry and nuclear magnetic resonance (NMR) revealed glyceroglycolipid and unique mannosyl fatty acids linked to mannitol as two Mincle ligands. An O -linked mannobiose-rich glycoprotein was identified as a Malassezia ligand for Dectin-2. Cytokine production in response to the Mincle ligands and the Dectin-2 ligand was abrogated in Mincle −/− and Dectin-2 −/− dendritic cells, respectively. These results demonstrate that Mincle and Dectin-2 recognize distinct ligands in Malassezia to induce host immune responses.

Mincle (also called as Clec4e or Clecsf9) is a C-type lectin receptor expressed in activated macrophages. Recently, we have reported that Mincle transduces the activation signals through ITAM-containing adaptor protein, FcRg, and induces the secretion of inflammatory cytokines. Furthermore, we and other groups have identified that Mincle recognizes a wide variety of ligands such as damaged cells, fungus, yeast and mycobacteria. These results indicate that Mincle acts as a multi-task danger receptor for both self and nonself ligands. This review summarizes the recent discoveries about the ligands and immunological roles of Mincle.

Tuberculosis remains a fatal disease caused by Mycobacterium tuberculosis, which contains various unique components that affect the host immune system. Trehalose-6,6′-dimycolate (TDM; also called cord factor) is a mycobacterial cell wall glycolipid that is the most studied immunostimulatory component of M. tuberculosis. Despite five decades of research on TDM, its host receptor has not been clearly identified. Here, we demonstrate that macrophage inducible C-type lectin (Mincle) is an essential receptor for TDM. Heat-killed mycobacteria activated Mincle-expressing cells, but the activity was lost upon delipidation of the bacteria; analysis of the lipid extracts identified TDM as a Mincle ligand. TDM activated macrophages to produce inflammatory cytokines and nitric oxide, which are completely suppressed in Mincle-deficient macrophages. In vivo TDM administration induced a robust elevation of inflammatory cytokines in sera and characteristic lung inflammation, such as granuloma formation. However, no TDM-induced lung granuloma was formed in Mincle-deficient mice. Whole mycobacteria were able to activate macrophages even in MyD88-deficient background, but the activation was significantly diminished in Mincle/MyD88 double-deficient macrophages. These results demonstrate that Mincle is an essential receptor for the mycobacterial glycolipid, TDM.