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1. (Article ID: 8565)
 
Huang HR, Li F, Han H, Xu X, Li N, Wang S, Xu JF, Jia XM
Dectin-3 recognizes glucuronoxylomannan of Cryptococcus neoformans serotype AD and Cryptococcus gattii serotype B to initiate host defense against Cryptococcosis
Frontiers in Immunology 9 (2018) 1781 (1-17)
 

Cryptococcus neoformans and Cryptococcus gattii cause life-threatening meningoencephalitis or lung diseases in immunocompetent individuals or immunocompromised ones. C. neoformans and C. gattii are subdivided into five serotypes based on their capsular glucuronoxylomannan (GXM). C. neoformans consists of serotypes A, D, and AD hybrid, and C. gattii consists of serotypes B and C. Given structural differences of GXM between C. neoformans and C. gattii, it remains unclear that how innate immune system recognizes GXM. Here, we report that C-type lectin receptor Dectin-3 (MCL encoded by Clec4d) is a direct receptor for GXMs from C. neoformans serotype AD (C.n-AD) and C. gattii serotype B (C.g-B). GXMs from C.n-AD and C.g-B activated NF-κB and ERK pathways to induce pro-inflammatory cytokine production, whereas it was completely abolished due to deficiency of Dectin-3 or caspase recruitment domain family member 9 (CARD9). Upon pulmonary C.n-AD and C.g-B infection, Dectin-3- and CARD9-deficient mice were highly susceptible and showed augmented lung injury due to impairment of alveolar macrophage accumulation and killing activities. Our study provides the first biological and genetic evidence demonstrating that Dectin-3 recognizes GXM of C.n-AD and C.g-B to initiate host defense against cryptococcosis.

innate immunity, Glucuronoxylomannan, C-type lectin receptor, Crytococcus, Dectin-3

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2. (Article ID: 8867)
 
Bie Q, Chen C, Yu M, Guo J, Wang J, Liu J, Zhou Y, Zhu H, Zhang Y
Dongtingnoids A−G: fusicoccane diterpenoids from a Penicillium species
Journal of Natural Products 82(1) (2019) 80-86
 

Five new diterpenoid glycosides, dongtingnoids A-E (1-5), two new diterpenoid aglycones, dongtingnoids F and G (6 and 7), and two known analogues, cotylenins E and J (8 and 9), belonging to the fusicoccane family, were isolated from the fungus Penicillium sp. DT10, which was derived from wetland soil from Dongting Lake. Their structures and absolute configurations were elucidated based on spectroscopic analyses, acid hydrolysis, ECD calculations, and X-ray crystallography. Dongtingnoid C (3) is the first 16-nor-fusicoccane diterpenoid glycoside reported and is proposed to form by oxidative demethylation. Compounds 1, 4, and 5 showed comparable seed-germination-promoting activities to that previously reported for the growth regulator cotylenin E (8).

seed germination, Penicillium, diterpenoid

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3. (Article ID: 8868)
 
Camoni L, Visconti S, Aducci P, Marra M
From plant physiology to pharmacology: fusicoccin leaves the leaves
Planta 249 (2019) 49–57
 

This review highlights 50 years of research on the fungal diterpene fusicoccin, during which the molecule went from a tool in plant physiology research to a pharmacological agent in treating animal diseases. Fusicoccin is a phytotoxic glycosylated diterpene produced by the fungus Phomopsis amygdali, a pathogen of almond and peach plants. Widespread interest in this molecule started when it was discovered that it is capable of causing stomate opening in all higher plants, thereby inducing wilting of leaves. Thereafter, FC became, and still is, a tool in plant physiology, due to its ability to influence a number of fundamental processes, which are dependent on the activation of the plasma membrane H+-ATPase. Molecular studies carried out in the last 20 years clarified details of the mechanism of proton pump stimulation, which involves the fusicoccin-mediated irreversible stabilization of the complex between the H+-ATPase and activatory 14-3-3 proteins. More recently, FC has been shown to influence cellular processes involving 14-3-3 binding to client proteins both in plants and animals. In this review, we report the milestones achieved in more than 50 years of research in plants and highlight recent advances in animals that have allowed this diterpene to be used as a 14-3-3 targeted drug.

Drug design, 14-3-3 proteins, protein–protein interaction, diterpene phytotoxin, Plasma membrane H+-ATPase

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