Figure 1.
Characterization of human monoclonal anti‐M antibody (S30) and analysis of glycosylation of SARS‐CoV M. (A) Proteins of purified SARS‐CoV were separated by 10% SDS–PAGE, and subjected to Western blot analysis using human serum (lane 1) or anti‐M antibody S30 (lane 2). (B) Purified viral proteins were treated with Endo H or PNGase F, and subjected to SDS–PAGE and Western Blot analysis using S30‐antibody as described above. Lane 1, purified SARS‐CoV without treatment; lanes 2 and 3, SARS‐CoV digested with Endo H or PNGase F, respectively. (C) M and the mutated MN4Q were in vitro translated in the presence (lanes 2 and 3) or absence (lane 1) of microsomal membranes. Immunoprecipitation was performed using S30‐antibody (lane 4). (D) M was in vitro translated in the presence of pancreatic microsomes and membrane‐bound proteins were treated without (lane 1), with proteinase K (lane 2), and with proteinase K and 1% Triton X‐100 (lane 3) and the samples were subjected to SDS–PAGE.