Protein Glycosylation and Myristylation in Chlorella Virus PBCV-1 and Its Antigenic Variants

Quideng Que, Yu Li, Ing Nang Wang, Leslie C. Lane, William G. Chaney, James L. Van Etten

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Chlorella virus PBCV-1 particles contain three glycoproteins, the major capsid protein Vp54 and two minor proteins Vp280 and Vp260. The major capsid protein is myristylated as well as glycosylated. Both modifications are in the carboxyl-terminal portion of the protein. A gene which is modified in a PBCV-1 antiserum-resistant mutant was cloned and sequenced. This gene has an open reading frame of 3099 bases and encodes one of the two large virion glycoproteins (Vp260). Vp260 contains 13 tandem repeats of 61 to 65 amino acids. The mutation deletes the equivalent of four of the amino acid repeat sequences and duplicates one of these sequences.

Original languageEnglish (US)
Article number71490
Pages (from-to)320-327
Number of pages8
JournalVirology
Volume203
Issue number2
DOIs
StatePublished - Sep 1994

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Chlorella
Capsid Proteins
Glycosylation
Amino Acid Repetitive Sequences
Glycoproteins
Viruses
Tandem Repeat Sequences
Virion
Open Reading Frames
Genes
Immune Sera
Proteins
Amino Acids
Mutation

ASJC Scopus subject areas

  • Virology

Cite this

Protein Glycosylation and Myristylation in Chlorella Virus PBCV-1 and Its Antigenic Variants. / Que, Quideng; Li, Yu; Wang, Ing Nang; Lane, Leslie C.; Chaney, William G.; Van Etten, James L.

In: Virology, Vol. 203, No. 2, 71490, 09.1994, p. 320-327.

Research output: Contribution to journalArticle

Que, Quideng ; Li, Yu ; Wang, Ing Nang ; Lane, Leslie C. ; Chaney, William G. ; Van Etten, James L. / Protein Glycosylation and Myristylation in Chlorella Virus PBCV-1 and Its Antigenic Variants. In: Virology. 1994 ; Vol. 203, No. 2. pp. 320-327.
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