scholarly journals Unconventional Secretion of Nigerolysins A from Aspergillus Species

2020 ◽  
Vol 8 (12) ◽  
pp. 1973
Author(s):  
Nada Kraševec ◽  
Maruša Novak ◽  
Simona Barat ◽  
Matej Skočaj ◽  
Kristina Sepčić ◽  
...  
Keyword(s):  
Bioinformatics Analysis ◽  
Specific Interaction ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Aspergillus Species ◽  
Unconventional Secretion ◽  
Alignment Analysis ◽  
Lipid Binding Proteins ◽  
Specific Membrane ◽  
Chromosomal Loci

Aegerolysins are small lipid-binding proteins particularly abundant in fungi. Aegerolysins from oyster mushrooms interact with an insect-specific membrane lipid and, together with MACPF proteins produced by the same organism, form pesticidal pore-forming complexes. The specific interaction with the same membrane lipid was recently demonstrated for nigerolysin A2 (NigA2), an aegerolysin from Aspergillus niger. In Aspergillus species, the aegerolysins were frequently found as secreted proteins, indicating their function in fungal defense. Using immunocytochemistry and live-cell imaging we investigated the subcellular localization of the nigerolysins A in A. niger, while their secretion was addressed by secretion prediction and Western blotting. We show that both nigerolysins A are leaderless proteins that reach the cell exterior by an unconventional protein secretion. NigA proteins are evenly distributed in the cytoplasm of fungal hyphae. A detailed bioinformatics analysis of Aspergillus aegerolysins suggests that the same function occurs only in a limited number of aegerolysins. From alignment, analysis of chromosomal loci, orthology, synteny, and phylogeny it follows that the same or a similar function described for pairs of pesticidal proteins of Pleurotus sp. can be expected in species of the subgenus Circumdati, section Nigri, series Nigri, and some other species with adjacent pairs of putative pesticidal proteins.

scholarly journals Lipid-Binding Aegerolysin from Biocontrol Fungus Beauveria bassiana

Toxins ◽  
2021 ◽  
Vol 13 (11) ◽  
pp. 820
Author(s):  
Nada Kraševec ◽  
Anastasija Panevska ◽  
Špela Lemež ◽  
Jaka Razinger ◽  
Kristina Sepčić ◽  
...  
Keyword(s):  
Beauveria Bassiana ◽  
Entomopathogenic Fungi ◽  
Bioinformatics Analysis ◽  
Membrane Attack Complex ◽  
Membrane Lipid ◽  
Antagonistic Activity ◽  
Lipid Binding ◽  
Biologically Relevant ◽  
Transmembrane Pores ◽  
Attack And Defense

Fungi are the most common pathogens of insects and thus important regulators of their populations. Lipid-binding aegerolysin proteins, which are commonly found in the fungal kingdom, may be involved in several biologically relevant processes including attack and defense against other organisms. Aegerolysins act alone or together with membrane-attack-complex/perforin (MACPF)-like proteins to form transmembrane pores that lead to cell lysis. We performed an in-depth bioinformatics analysis of aegerolysins in entomopathogenic fungi and selected a candidate aegerolysin, beauveriolysin A (BlyA) from Beauveria bassiana. BlyA was expressed as a recombinant protein in Escherichia coli, and purified to further determine its functional and structural properties, including lipid-binding ability. Aegerolysins were found to be encoded in genomes of entomopathogenic fungi, such as Beauveria, Cordyceps, Metarhizium and Ophiocordyceps. Detailed bioinformatics analysis revealed that they are linked to MACPF-like genes in most genomes. We also show that BlyA interacts with an insect-specific membrane lipid. These results were placed in the context of other fungal and bacterial aegerolysins and their partner proteins. We believe that aegerolysins play a role in promoting the entomopathogenic and antagonistic activity of B. bassiana, which is an active ingredient of bioinsecticides.

scholarly journals MCE domain proteins: conserved inner membrane lipid-binding proteins required for outer membrane homeostasis

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Georgia L. Isom ◽  
Nathaniel J. Davies ◽  
Zhi-Soon Chong ◽  
Jack A. Bryant ◽  
Mohammed Jamshad ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Binding Proteins ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Inner Membrane ◽  
Lipid Binding Proteins

scholarly journals MBPpred: Proteome-wide detection of membrane lipid-binding proteins using profile Hidden Markov Models

2015 ◽  
Author(s):  
Katerina C. Nastou ◽  
Georgios N. Tsaousis ◽  
Nikolaos C. Papandreou ◽  
Stavros J. Hamodrakas
Keyword(s):  
Binding Proteins ◽  
Markov Models ◽  
Membrane Lipids ◽  
Hidden Markov ◽  
Membrane Binding ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Binding Domains ◽  
Eukaryotic Proteomes ◽  
Lipid Binding Proteins

ABSTRACTA large number of modular domains that exhibit specific lipid binding properties are present in many membrane proteins involved in trafficking and signal transduction. These domains are present in either eukaryotic peripheral membrane or transmembrane proteins and are responsible for the non-covalent interactions of these proteins with membrane lipids. Here we report a profile Hidden Markov Model based method capable of detecting Membrane Binding Proteins (MBPs) from information encoded in their amino acid sequence, called MBPpred. The method identifies MBPs that contain one or more of the Membrane Binding Domains (MBDs) that have been described to date, and further classifies these proteins based on their position in respect to the membrane, either as peripheral or transmembrane. MBPpred is available online at http://bioinformatics.biol.uoa.gr/MBPpred. This method was applied in selected eukaryotic proteomes, in order to examine the characteristics they exhibit in various eukaryotic kingdoms and phylums.

scholarly journals MCE domain proteins: conserved inner membrane lipid-binding proteins required for outer membrane homeostasis

2017 ◽  
Author(s):  
Georgia L. Isom ◽  
Nathaniel J. Davies ◽  
Zhi-Soon Chong ◽  
Jack A. Bryant ◽  
Mohammed Jamshad ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Cell Envelope ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Single Domain ◽  
Inner Membrane ◽  
Bacterial Phyla ◽  
Single Domain Protein ◽  
Lipid Binding Proteins

Bacterial proteins with MCE domains were first described as being important forMammalianCellEntry. More recent evidence suggests they are components of lipid ABC transporters. InEscherichia coli, the single-domain protein MlaD is known to be part of an inner membrane transporter that is important for maintenance of outer membrane lipid asymmetry. Here we describe two multi MCE domain-containing proteins inEscherichia coli, PqiB and YebT, the latter of which is an orthologue of MAM-7 that was previously reported to be an outer membrane protein. We show that all three MCE domain-containing proteins localise to the inner membrane. Bioinformatic analyses revealed that MCE domains are widely distributed across bacterial phyla but multi MCE domain-containing proteins evolved in Proteobacteria from single-domain proteins. Mutants defective inmlaD,pqiABandyebSTwere shown to have distinct but partially overlapping phenotypes, but the primary functions of PqiB and YebT differ from MlaD. Complementing our previous findings that all three proteins bind phospholipids, results presented here indicate that multi-domain proteins evolved in Proteobacteria for specific functions in maintaining cell envelope homeostasis.

scholarly journals Triple-Knockout, Synuclein-Free Mice Display Compromised Lipid Pattern

Molecules ◽  
2021 ◽  
Vol 26 (11) ◽  
pp. 3078
Author(s):  
Irina A. Guschina ◽  
Natalia Ninkina ◽  
Andrei Roman ◽  
Mikhail V. Pokrovskiy ◽  
Vladimir L. Buchman
Keyword(s):  
Fatty Acids ◽  
Lipid Metabolism ◽  
Family Members ◽  
Ether Lipid ◽  
Brain Regions ◽  
Membrane Lipid ◽  
Lipid Binding ◽  
Synaptic Functions ◽  
Ethanolamine Plasmalogens ◽  
Lipid Pattern

Recent studies have implicated synucleins in several reactions during the biosynthesis of lipids and fatty acids in addition to their recognised role in membrane lipid binding and synaptic functions. These are among aspects of decreased synuclein functions that are still poorly acknowledged especially in regard to pathogenesis in Parkinson’s disease. Here, we aimed to add to existing knowledge of synuclein deficiency (i.e., the lack of all three family members), with respect to changes in fatty acids and lipids in plasma, liver, and two brain regions in triple synuclein-knockout (TKO) mice. We describe changes of long-chain polyunsaturated fatty acids (LCPUFA) and palmitic acid in liver and plasma, reduced triacylglycerol (TAG) accumulation in liver and non-esterified fatty acids in plasma of synuclein free mice. In midbrain, we observed counterbalanced changes in the relative concentrations of phosphatidylcholine (PC) and cerebrosides (CER). We also recorded a notable reduction in ethanolamine plasmalogens in the midbrain of synuclein free mice, which is an important finding since the abnormal ether lipid metabolism usually associated with neurological disorders. In summary, our data demonstrates that synuclein deficiency results in alterations of the PUFA synthesis, storage lipid accumulation in the liver, and the reduction of plasmalogens and CER, those polar lipids which are principal compounds of lipid rafts in many tissues. An ablation of all three synuclein family members causes more profound changes in lipid metabolism than changes previously shown to be associated with γ-synuclein deficiency alone. Possible mechanisms by which synuclein deficiency may govern the reported modifications of lipid metabolism in TKO mice are proposed and discussed.

The role of dynamics in modulating ligand exchange in intracellular lipid binding proteins

2014 ◽  
Vol 1844 (7) ◽  
pp. 1268-1278 ◽  
Author(s):  
Laura Ragona ◽  
Katiuscia Pagano ◽  
Simona Tomaselli ◽  
Filippo Favretto ◽  
Alberto Ceccon ◽  
...  
Keyword(s):  
Ligand Exchange ◽  
Binding Proteins ◽  
Lipid Binding ◽  
Intracellular Lipid ◽  
Lipid Binding Proteins

scholarly journals INTRACELLULAR LIPID-BINDING PROTEINS AND THEIR GENES

1997 ◽  
Vol 17 (1) ◽  
pp. 277-303 ◽  
Author(s):  
David A. Bernlohr ◽  
Melanie A. Simpson ◽  
Ann Vogel Hertzel ◽  
Leonard J. Banaszak
Keyword(s):  
Binding Proteins ◽  
Lipid Binding ◽  
Intracellular Lipid ◽  
Lipid Binding Proteins
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