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Article

N-Terminal segment of potato virus X coat protein subunits is glycosylated and mediates formation of a bound water shell on the virion surface.

European journal of biochemistry - 1 Aug 2004

Baratova Lyudmila A, Fedorova Nataliya V, Dobrov Eugenie N, Lukashina Elena V, Kharlanov Andrey N, Nasonov Vitaly V, Serebryakova Marina V, Kozlovsky Stanislav V, Zayakina Olga V, Rodionova Nina P

Abstract excerpt

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...

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PMID: 15265033
DOI: 10.1111/j.1432-1033.2004.04243.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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