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. 2005 Mar 29;579(11):2387–2396. doi: 10.1016/j.febslet.2005.03.039

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FEBS Letters 579 (2005) 1873-3468 © 2015 Federation of European Biochemical Societies

This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.

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figure image — Further analysis of the homo‐oligomerization of SARS‐C‐V N protein. (A) HeLa cells overexpressing the empty pKT0‐Flag (lane 1), wild type N protein (lane 2), or the K62A mutant N protein (lane 3) were lysed in the presence of IAA and NEM. The lysates were immunoprecipitated with anti‐Flag antibody. The precipitated polypeptides were separated by SDS–PAGE under nonreducing conditions and analyzed by Western blotting with anti‐Flag antibody. The three major isoforms of N protein, the N protein dimer, and the immunoglobulin are indicated. Numbers on the left indicate molecular masses in kilodaltons. (B) HeLa cells overexpressing the Flag‐tagged wild type N protein alone (lane 1), the c‐Myc‐tagged wild type N protein alone (lane 2), the Flag‐tagged wild type and c‐Myc‐tagged wild type N protein (lane 3), and the Flag‐tagged K62A mutant and c‐Myc‐tagged wild type N protein (lane 4) were lysed in the presence of IAA and NEM. Polypeptides were immunoprecipitated with anti‐Myc antibody, separated by SDS–PAGE under nonreducing conditions, and analyzed by Western blotting with anti‐Flag antibody. The N protein dimer and the immunoglobulin are indicated. A band migrating at approximately 50 kDa, which may represent the antibody heavy chain, is also indicated. (C) HeLa cells overexpressing the Flag‐tagged wild type N protein alone (lanes 1 and 5), the c‐Myc‐tagged wild type N protein alone (lanes 2 and 6), the Flag‐tagged wild type and c‐Myc‐tagged wild type N protein (lanes 3 and 7), and the Flag‐tagged K62A mutant and c‐Myc‐tagged wild type N protein (lanes 4 and 8) were lysed in the presence of IAA and NEM. Polypeptides were separated by SDS–PAGE under nonreducing conditions, and analyzed by Western blotting with either anti‐Flag antibody (lanes 1–4), or anti‐Myc antibody (lanes 5–8). The three major isoforms of N protein and the dimer are indicated.