Kwak Eun-A, Jaworski Justyn
Hanyang University, 222 Wangsimni-ro, Seongdong-gu, Seoul, S. Korea.
J Mater Chem B. 2013 Jul 28;1(28):3486-3493. doi: 10.1039/c3tb20526f. Epub 2013 Jun 6.
A unique method for the controlled attachment of viruses (or other protein based materials) to a range of surfaces is revealed through site-specific linkages engineered at the fd phage p3 protein coat. After genetic encoding of the virus coat position that is to be engineered, enzymatic modification with a formylglycine generating enzyme (FGE) affords the conversion of a single amino acid at a precise location to yield a reactive aldehyde group. By implementing this modification at a specific p3 coat position, we demonstrate the ability to control the directed immobilization of the virus selectively onto amine exposed surfaces including APTES treated glass, polymeric supports, and protein coated magnetic beads. While the immobilized virus remains stable for even a month, we also show by controlled release from the surface that liberated viruses retain their infectivity. The adaptability of this modification strategy for virus engineering is demonstrated showing great potential for bioconjugation with a range of amine functionalized chemical targets. This is expected to greatly enhance the possibilities for future virus based materials and related technologies.
通过在fd噬菌体p3蛋白衣壳上设计位点特异性连接，揭示了一种将病毒（或其他基于蛋白质的材料）可控附着到一系列表面的独特方法。在对要进行工程改造的病毒衣壳位置进行基因编码后，用甲酰甘氨酸生成酶（FGE）进行酶促修饰，可将精确位置的单个氨基酸转化为反应性醛基。通过在特定的p3衣壳位置进行这种修饰，我们展示了将病毒选择性地定向固定到胺暴露表面的能力，这些表面包括经APTES处理的玻璃、聚合物载体和蛋白质包被的磁珠。虽然固定化的病毒即使在一个月内仍保持稳定，但我们还通过从表面控制释放表明，释放出的病毒保留了它们的感染性。这种修饰策略在病毒工程中的适应性得到了证明，显示出与一系列胺功能化化学靶标进行生物共轭的巨大潜力。预计这将大大增加未来基于病毒的材料和相关技术的可能性。
