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10.1134/S0006297918080096 http://scihub22266oqcxt.onion/10.1134/S0006297918080096 30208834!ä!30208834 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=30208834&cmd=llinks): Failed to open stream: HTTP request failed! 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Amphipathic CRAC-Containing Peptides Derived from the Influenza Virus A M1 Protein Modulate Cholesterol-Dependent Activity of Cultured IC-21 Macrophages |pdf=|usr=}}{{30208834}} gab.com Text Amphipathic CRAC-Containing Peptides Derived from the Influenza Virus A M1 Protein Modulate Cholesterol-Dependent Activity of Cultured IC-21 Macrophages JO: Biochemistry (Mosc) http://www.kidney.de/pget.php?&tw=1&pmid=30208834 #FOAvip Entry of many viral and bacterial pathogens into host cells depends on cholesterol and/or cholesterol-enriched domains (lipid rafts) in the cell membrane. Earlier, we showed that influenza virus A matrix protein M1 contains amphipathic alpha-helices with exposed cholesterol-recognizing amino acid consensus (CRAC) motifs. In order to test possible functional activity of these motifs, we studied the effects of three synthetic peptides corresponding to the CRAC-containing alpha-helices of the viral M1 protein on the phagocytic activity of cultured mouse IC-21 macrophages. The following peptides were used: LEVLMEWLKTR (M1 alpha-helix 3, a.a. 39-49; further referred to as peptide 1), NNMDKAVKLYRKLK (M1 alpha-helix 6, a.a. 91-105; peptide 2), and GLKNDLLENLQAYQKR (M1 alpha-helix 13, a.a. 228-243; peptide 3). We found that all three peptides modulated interactions of IC-21 macrophages with non-opsonized 2-microm target particles. The greatest effect was demonstrated by peptide 2: in the presence of 35 muM peptide 2, the phagocytic index of IC-21 macrophages exceeded the control value by 60%; 10-11 mM methyl-beta-cyclodextrin abolished this effect. Peptides 1 and 3 exerted weak inhibitory effect in a narrow concentration range of 5-10 muM. The dose-response curves could be approximated by a sum of two (stimulatory and inhibitory) components with different Hill coefficients, suggesting existence of at least two peptide-binding sites with different affinities on the cell surface. CD spectroscopy confirmed that the peptides exhibit structural flexibility in solutions. Altogether, our data indicate that amphipathic CRAC-containing peptides derived from the viral M1 protein modulate lipid raft-dependent processes in IC-21 macrophages. Twit Text FOAVip Amphipathic CRAC-Containing Peptides Derived from the Influenza Virus A M1 Protein Modulate Cholesterol-Dependent Activity of Cultured IC-21 Macrophages ????Biochemistry (Mosc) http://www.kidney.de/pget.php?&tw=1&pmid=30208834 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30208834 #FOAvip English Wikipedia <ref>{{Cite pmid|30208834}}</ref> Amphipathic CRAC-Containing Peptides Derived from the Influenza Virus A M1 Protein Modulate Cholesterol-Dependent Activity of Cultured IC-21 Macrophages #MMPMID30208834 Dunina-Barkovskaya AY; Vishnyakova KS; Golovko AO; Arutyunyan AM; Baratova LA; Bathishchev OV; Radyukhin VA Biochemistry (Mosc) 2018[Aug]; 83 (8): 982-991 PMID30208834show ga Entry of many viral and bacterial pathogens into host cells depends on cholesterol and/or cholesterol-enriched domains (lipid rafts) in the cell membrane. Earlier, we showed that influenza virus A matrix protein M1 contains amphipathic alpha-helices with exposed cholesterol-recognizing amino acid consensus (CRAC) motifs. In order to test possible functional activity of these motifs, we studied the effects of three synthetic peptides corresponding to the CRAC-containing alpha-helices of the viral M1 protein on the phagocytic activity of cultured mouse IC-21 macrophages. The following peptides were used: LEVLMEWLKTR (M1 alpha-helix 3, a.a. 39-49; further referred to as peptide 1), NNMDKAVKLYRKLK (M1 alpha-helix 6, a.a. 91-105; peptide 2), and GLKNDLLENLQAYQKR (M1 alpha-helix 13, a.a. 228-243; peptide 3). We found that all three peptides modulated interactions of IC-21 macrophages with non-opsonized 2-microm target particles. The greatest effect was demonstrated by peptide 2: in the presence of 35 muM peptide 2, the phagocytic index of IC-21 macrophages exceeded the control value by 60%; 10-11 mM methyl-beta-cyclodextrin abolished this effect. Peptides 1 and 3 exerted weak inhibitory effect in a narrow concentration range of 5-10 muM. The dose-response curves could be approximated by a sum of two (stimulatory and inhibitory) components with different Hill coefficients, suggesting existence of at least two peptide-binding sites with different affinities on the cell surface. CD spectroscopy confirmed that the peptides exhibit structural flexibility in solutions. Altogether, our data indicate that amphipathic CRAC-containing peptides derived from the viral M1 protein modulate lipid raft-dependent processes in IC-21 macrophages. |*Consensus Sequence[MESH] |*Hydrophobic and Hydrophilic Interactions[MESH] |Amino Acid Motifs[MESH] |Amino Acid Sequence[MESH] |Animals[MESH] |Cells, Cultured[MESH] |Cholesterol/*metabolism[MESH] |Macrophages/cytology/*metabolism[MESH] |Mice[MESH] |Peptide Fragments/*chemistry/*metabolism[MESH] |Phagocytosis[MESH]Amphipathic CRAC-Containing Peptides Derived from the Influenza Virus (epmc).pdf DeepDyve Pubget Overpricing