Adsorption and aggregation properties of norovirus GI and GII virus-like particles demonstrate differing responses to solution chemistry.

Adsorption and aggregation properties of norovirus GI and GII virus-like particles demonstrate differing responses to solution chemistry.
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DOI:
10.1021/es102368d
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发表时间:
2011-01-15
影响因子:
11.4
通讯作者:
Elimelech, Menachem
Elimelech, Menachem
中科院分区:
环境科学与生态学1区
文献类型:
--
作者:
da Silva, Allegra K.;Kavanagh, Owen V.;Estes, Mary K.;Elimelech, Menachem

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本文研究了诺沃克(Norwalk)GII.1和休斯敦(Houston)GII.4两株诺如病毒的病毒样颗粒(VLP)在不同溶液中的吸附和聚集行为。发现GI. 1和GII. 4 VLP在pH 4.0-8.0下抗聚集稳定。在pH 9.0时,GI. 1 VLP迅速崩解。在pH 8.0的NaCl溶液中,GI. 1和GII. 4 VLP对二氧化硅的附着效率(α)随着离子强度的增加而增加。GI. 1 VLP的附着效率随着pH增加而降低,高于等电点(pH 5.0),而在等电点和低于等电点时,附着效率是不稳定的。Ca 2+和Mg 2+显著增加了GI. 1和GII. 4 VLP的附着效率,这可能是由于与VLP衣壳的特异性相互作用。双环戊二烯基降低了GI.1和GII.4 VLP的附着效率,而磷酸盐降低了GI.1的附着效率,同时增加了GII.4的附着效率。在响应于溶液化学的GI. 1和GII. 4 VLP附着效率中观察到的差异可归因于每个VLP菌株的衣壳表面上暴露的氨基酸残基的独特排列的差异响应。
The transport properties (adsorption and aggregation behavior) of virus-like particles (VLPs) of two strains of norovirus (“Norwalk” GI.1 and “Houston” GII.4) were studied in a variety of solution chemistries. GI.1 and GII.4 VLPs were found to be stable against aggregation at pH 4.0–8.0. At pH 9.0, GI.1 VLPs rapidly disintegrated. The attachment efficiencies (α) of GI.1 and GII.4 VLPs to silica increased with increasing ionic strength in NaCl solutions at pH 8.0. The attachment efficiency of GI.1 VLPs decreased as pH was increased above the isoelectric point (pH 5.0), whereas at and below the isoelectric point, the attachment efficiency was erratic. Ca2+ and Mg2+ dramatically increased the attachment efficiencies of GI.1 and GII.4 VLPs, which may be due to specific interactions with the VLP capsids. Bicarbonate decreased attachment efficiencies for both GI.1 and GII.4 VLPs, whereas phosphate decreased the attachment efficiency of GI.1, while increasing GII.4 attachment efficiency. The observed differences in GI.1 and GII.4 VLP attachment efficiencies in response to solution chemistry may be attributed to differential responses of the unique arrangement of exposed amino acid residues on the capsid surface of each VLP strain.
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