Destruxins (DTXs) are cyclic peptide toxins secreted by the entomopathogenic fungus Metarhizium anisopliae var. anisopliae. The effects of DTX E, the most active compound of this family on haemocytes, the immunocompetent insect cells, and on the dynamics and efficacy of the multicellular defense of insect hosts have been investigated. Ultrastructural alterations have been observed in circulating plasmatocytes and granular haemocytes, and in attached haemocytes of Galleria mellonella larvae treated with a toxic dose of DTX E (LC50). These changes appear as a consequence of disturbances induced in the cellular calcium balance. An effect on the cell surface of granulocytes was also noted in cells incubated with the toxin and FITC-Con A, even when the concentration of DTX was as low as 0.005 microg/ml. Morphological studies of haemocytic capsules formed in vivo revealed disturbances of the multicellular defense mechanism after toxin treatment However, an attempt to establish if these changes were significant was unsuccessful. In contrast, comparative assays regarding the effect of toxin treatment on the efficacy of the antifungal effect of encapsulation has given conclusive results. The germination of injected Aspergillus niger spores became slightly but significantly increased, and when the granuloma were incubated the fungus escaped more easily from the haemocytic envelope. These results are discussed in terms of significance of the contribution of DTXs to the fungal infection process. It is suggested that the fungal peptides may intervene during the disease by a true immune-inhibitory effect occurring at doses which do not cause paralysis or any general sign of toxicity (e.g., 0.8 microg/g of body weight).
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http://dx.doi.org/10.1016/s0022-2011(02)00104-0 | DOI Listing |
Sci Adv
January 2025
Institut für Biologie und Biotechnologie der Pflanzen, Universität Münster, Münster, Germany.
Systemic signaling is an essential hallmark of multicellular life. Pathogen encounter occurs locally but triggers organ-scale and organismic immune responses. In plants, elicitor perception provokes systemically expanding Ca and HO signals conferring immunity.
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January 2025
Department of Biochemistry, Faculty of Biology and Biotechnology, University of Warmia and Mazury in Olsztyn, Oczapowskiego 1A, Olsztyn, 10-719, Poland.
Multicellular animals need to control the spread of invading pathogens. This is a particular challenge for blood-feeding vectors such as ticks, which ingest large amounts of blood potentially laden with harmful microorganisms. Ticks have a basic innate immune system and protect themselves from infection through innate immune responses involving pathways such as Janus kinase (JAK) or the signalling transducer activator of transcription (STAT).
View Article and Find Full Text PDFPlant Physiol
December 2024
Instituto de Bioingeniería, Universidad Miguel Hernández, Campus de Elche, 03202 Elche, Alicante, Spain.
Zinc knuckle (ZCCHC) motif-containing proteins are present in unicellular and multicellular eukaryotes, and most ZCCHC proteins with known functions participate in the metabolism of various classes of RNA, such as mRNAs, ribosomal RNAs, and microRNAs. The Arabidopsis (Arabidopsis thaliana) genome encodes 69 ZCCHC-containing proteins; however, the functions of most remain unclear. One of these proteins, CAX-INTERACTING PROTEIN 4 (CXIP4, encoded by AT2G28910), has been classified as a PTHR31437 family member.
View Article and Find Full Text PDFInt J Biol Sci
December 2024
Division of Science Education, Kangwon National University, 24341, Republic of Korea.
J Basic Microbiol
December 2024
Univ Lyon, Université Lyon1, CNRS, INSA-Lyon, Microbiologie, Adaptation et Pathogénie, Villeurbanne, France.
LysM effectors are suppressors of chitin-triggered plant immunity in biotrophic and hemibiotrophic fungi. In necrotrophic fungi, LysM effectors might induce a mechanism to suppress host immunity during the short asymptomatic phase they establish before these fungi activate plant defenses and induce host cell death leading to necrosis. Here, we characterize a secreted LysM protein from a major necrotrophic fungus, Botrytis cinerea, called BcLysM1.
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