Universal method for synthesis of artificial gel antibodies by the imprinting approach combined with a unique electrophoresis technique for detection of minute structural differences of proteins, viruses, and cells (bacteria): II. Gel antibodies against virus (Semliki Forest Virus)

• Published in: Journal of separation science Vol. 29; no. 18; pp. 2810 - 2815
• Main Authors: Takátsy, Anikó, Sedzik, Jan, Kilár, Ferenc, Hjertén, Stellan
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 01-12-2006; WILEY‐VCH Verlag; Wiley
• Subjects: Antibodies, Viral - chemistry; Artificial antibodies; Biological and medical sciences; Electrophoresis - methods; Free zone electrophoresis; Fundamental and applied biological sciences. Psychology; Imprinting; MEDICIN; Medicin och hälsovetenskap; MEDICINE; Microbiology; Recognition; Semliki Forest Virus; Semliki forest virus - immunology; Techniques used in virology; Virology; Semliki forest virus; Zone electrophoresis; Artificial antibodies; Antibody; Capillary electrophoresis; Togaviridae; Selectivity; Virus; Analysis method; Electrophoretic mobility; Acrylamide copolymer; Alphavirus; e zone electrophoresis / Imprinting / Recognition / Semliki Forest Virus; Mutation; Chemical synthesis; Molecular imprinting; Stationary phase
• ISSN: 1615-9306; 1615-9314; 1615-9314
• DOI: 10.1002/jssc.200600212

Artificial and highly selective antibodies (in the form of gel granules) against proteins can easily be synthesized by a simple, cost‐effective imprinting technique [Liao, J.‐L. et al., Chromatographia 1996, 42, 259–262]. Using the same method for synthesis of gel antibodies against viruses in combination with analysis by free zone electrophoresis in a rotating narrow bore tube we have shown that artificial gel antibodies against Semliki Forest Virus (wild type) can sense the difference between this virus and a mutant, although they differ in their chemical composition only by three amino acids in one of the three proteins on the surface of the virus particle. The reason for this extremely high resolution is explained by the fact that we use three types of selectivity: (i) shape selectivity (created by the close fit between the antigen and its imprint in the gel), (ii) bond selectivity in the contact area between the antigen and its imprint in the gel antibody, and (iii) charge selectivity, originating from slightly different structures or/and conformations of the antigens.