TAILIEUCHUNG - Báo cáo khoa học: N-Terminal segment of potato virus X coat protein subunits is glycosylated and mediates formation of a bound water shell on the virion surface

The primary structures of N-terminal 19-mer peptides, released by limited trypsin treatment of coat protein (CP) subunits in intact virions of three potato virus X (PVX) isolates, were analyzed. Twowild-type PVXstrains,Russian (Ru) andBritish (UK3),wereusedandalso theSTmutantof UK3 inwhich all 12 serine and threonine residues in the CP N-terminal segment were replaced by glycine or alanine. | Eur. J. Biochem. 271 3136-3145 2004 FEBS 2004 doi N-Terminal segment of potato virus X coat protein subunits is glycosylated and mediates formation of a bound water shell on the virion surface Lyudmila A. Baratova1 Nataliya V. Fedorova1 Eugenie N. Dobrov1 Elena V. Lukashina1 Andrey N. Kharlanov2 Vitaly V. Nasonov3 Marina V. Serebryakova4 Stanislav V. Kozlovsky1 Olga V. Zayakina1 and Nina P. Rodionova1 1A. N. Belozersky Institute of Physico-Chemical Biology Moscow State University Russia 2 Department of Chemistry Moscow State University Russia 3 M. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences Moscow Russia 4V. N. Orekhovich Institute of Biomedical Chemistry Russian Academy of Medical Sciences Moscow Russia The primary structures of N-terminal 19-mer peptides released by limited trypsin treatment of coat protein CP subunits in intact virions of three potato virus X PVX isolates were analyzed. Two wild-type PVX strains Russian Ru and British UK3 were used and also the ST mutant of UK3 in which all 12 serine and threonine residues in the CP N-terminal segment were replaced by glycine or alanine. With the help of direct carbohydrate analysis and MS it was found that the acetylated N-terminal peptides of both wildtype strains are glycosylated by a single monosaccharide residue galactose or fucose at NAcSer in the first position of the CP sequence whereas the acetylated N-terminal segment of the ST mutant CP is unglycosylated. Fourier transform infrared spectra in the 1000-4000 cm-1 region were measured for films of the intact and in situ trypsin-degraded PVX preparations at low and high humidity. These spectra revealed the presence of a broad-band in the region of valent vibrations of OH bonds 3100-3700 cm-1 which can be represented by superposition of three bands corresponding to tightly bound weakly bound and free OH groups. On calculating difference wet minus dry spectra it was found

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