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10.1016/j.virol.2014.04.004 http://scihub22266oqcxt.onion/10.1016/j.virol.2014.04.004 24889255!ä!24889255 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Virology 2014 ; 456-457 (ä): 364-9 Nephropedia Template TP {{tp|p=24889255|t=2014. Parvovirus B19 VLP recognizes globoside in supported lipid bilayers |pdf=|usr=}}{{24889255}} gab.com Text Parvovirus B19 VLP recognizes globoside in supported lipid bilayers JO: Virology http://www.kidney.de/pget.php?&tw=1&pmid=24889255 #FOAvip Studies have suggested that the glycosphingolipid globoside (Gb4Cer) is a receptor for human parvovirus B19. Virus-like particles bind to Gb4Cer on thin-layer chromatograms, but a direct interaction between the virus and lipid membrane-associated Gb4Cer has been debated. Here, we characterized the binding of parvovirus B19 VP1/VP2 virus-like particles to glycosphingolipids (i) on thin-layer chromatograms (TLCs) and (ii) incorporated into supported lipid bilayers (SLBs) acting as cell-membrane mimics. The binding specificities of parvovirus B19 determined in the two systems were in good agreement; the VLP recognized both Gb4Cer and the Forssman glycosphingolipid on TLCs and in SLBs compatible with the role of Gb4Cer as a receptor for this virus. Twit Text FOAVip Parvovirus B19 VLP recognizes globoside in supported lipid bilayers ????Virology http://www.kidney.de/pget.php?&tw=1&pmid=24889255 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24889255 #FOAvip English Wikipedia <ref>{{Cite pmid|24889255}}</ref> Parvovirus B19 VLP recognizes globoside in supported lipid bilayers #MMPMID24889255 Nasir W; Nilsson J; Olofsson S; Bally M; Rydell GE Virology 2014[May]; 456-457 (ä): 364-9 PMID24889255show ga Studies have suggested that the glycosphingolipid globoside (Gb4Cer) is a receptor for human parvovirus B19. Virus-like particles bind to Gb4Cer on thin-layer chromatograms, but a direct interaction between the virus and lipid membrane-associated Gb4Cer has been debated. Here, we characterized the binding of parvovirus B19 VP1/VP2 virus-like particles to glycosphingolipids (i) on thin-layer chromatograms (TLCs) and (ii) incorporated into supported lipid bilayers (SLBs) acting as cell-membrane mimics. The binding specificities of parvovirus B19 determined in the two systems were in good agreement; the VLP recognized both Gb4Cer and the Forssman glycosphingolipid on TLCs and in SLBs compatible with the role of Gb4Cer as a receptor for this virus. |*Virus Attachment[MESH] |Capsid Proteins/metabolism[MESH] |Globosides/*metabolism[MESH] |Lipid Bilayers/*metabolism[MESH] |Parvovirus B19, Human/*physiology[MESH] |Receptors, Virus/*metabolism[MESH]Parvovirus B19 VLP recognizes globoside in supported lipid bilayers (epmc).pdf DeepDyve Pubget Overpricing