Competition for Membrane Receptors: Norovirus Detachment via Lectin Attachment

被引:19
作者
Parveen, Nagma [1 ,8 ]
Rydell, Gustaf E. [2 ]
Larson, Goran [3 ]
Hytonen, Vesa P. [4 ,5 ,6 ]
Zhdanov, Vladimir P. [1 ,7 ]
Hook, Fredrik [1 ]
Block, Stephan [1 ,9 ]
机构
[1] Chalmers Univ Technol, Dept Phys, Gothenburg, Sweden
[2] Univ Gothenburg, Sahlgrenska Acad, Dept Infect Dis, Gothenburg, Sweden
[3] Univ Gothenburg, Sahlgrenska Acad, Dept Lab Med, Gothenburg, Sweden
[4] Tampere Univ, Fac Med & Hlth Technol, Tampere, Finland
[5] Tampere Univ, BioMediTech, Tampere, Finland
[6] Fimlab Labs, Tampere, Finland
[7] Russian Acad Sci, Boreskov Inst Catalysis, Novosibirsk, Russia
[8] Katholieke Univ Leuven, Dept Chem, Lab Photochem & Spect, Leuven, Belgium
[9] Free Univ Berlin, Dept Chem & Biochem, Berlin, Germany
基金
瑞典研究理事会; 芬兰科学院;
关键词
SUPPORTED LIPID-BILAYERS; SMALL-MOLECULE INHIBITOR; BLOOD-GROUP ANTIGENS; STRUCTURAL BASIS; VIRAL ENTRY; BINDING; VIRUS; PROTEIN; LIGAND; MODEL;
D O I
10.1021/jacs.9b06036
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Virus internalization into the host cells occurs via multivalent interactions, in which a single virus binds to multiple receptors in parallel. Because of analytical and experimental limitations this complex type of interaction is still poorly understood and quantified. Herein, the multivalent interaction of norovirus-like particles (noroVLPs) with H or B type 1 glycosphingolipids (GSLs), embedded in a supported phospholipid bilayer, is investigated by following the competition between noroVLPs and a lectin (from Ralstonia solanacearum) upon binding to these GSLs. Changes in noroVLP and lectin coverage, caused by competition, were monitored for both GSLs and at different GSL concentrations using quartz crystal microbalance with dissipation monitoring. The study yields information about the minimum GSL concentration needed for (i) noroVLPs to achieve firm attachment to the bilayer prior to competition and to (ii) remain firmly attached to the bilayer during competition. We show that these two concentrations are almost identical for the H type 1-noroVLP interaction but differ for B type 1, indicating an accumulation of B type 1 GSLs in the noroVLP-bilayer interaction area. Furthermore, the GSL concentration required for firm attachment is significantly larger for H type 1 than for B type 1, indicating a higher affinity of noroVLP toward B type 1. This finding is supported by extracting the energy of single noroVLP-H type 1 and noroVLP-B type 1 bonds from the competition kinetics, which were estimated to be 5 and 6 kcal/mol, respectively. This demonstrates the potential of utilizing competitive binding kinetics to analyze multivalent interactions, which has remained difficult to quantify using conventional approaches.
引用
收藏
页码:16303 / 16311
页数:9
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