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Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: An antigenic epitope of influenza virus nucleoprotein (NP) associated with polymeric forms of NP | Virology Journal BioMed Central Open Access Short report An antigenic epitope of influenza virus nucleoprotein NP associated with polymeric forms of NP Elena N Prokudina 1 Nataly Semenova1 Valery Chumakov1 and Lothar Stitz2 Address rrhe D.I. Ivanovsky Institute of Virology Gamaleya str. 16 Moscow Russia and 2Friedrich-Loeffler-Institut D-72076 Tubingen Germany Email Elena N Prokudina - prokudinaen@mail.ru Nataly Semenova - prokudina@virology.ru Valery Chumakov - prokudina@virology.ru Lothar Stitz - Lothar.Stitz@fli.bound.de Corresponding author Published 29 February 2008 Virology Journal 2008 5 37 doi 10.1 I86 I743-422X-5-37 Received 15 February 2008 Accepted 29 February 2008 This article is available from http www.virologyj.cOm content 5 1 37 2008 Prokudina et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Intracellular influenza virus nucleoprotein NP is characterized by a high efficiency of homopolymers formation however their antigenic structure is still incompletely known. Herein we report that RNase-resistant intracellular NP homo-polymers have a highly ordered conformational antigenic epitope which depends on inter-subunit interactions of monomeric NPs. Our studies have shown that in radioimmunoprecipitation RIPA intracellular NP polymers bind mAb N5D3 and RNase does not prevent their mAb binding. In contrast to NP polymers NP monomeric subunits obtained by thermo-dissociation of NP polymers fail to bind the mAb N5D3 in RIPA. At the same time the in vitro concentration of thermo-denatured monomeric NPs in both soluble and immobilized forms results in NP-NP association accompanied by renaturation of the N5D3 epitope. The same
