Identification of VP19 and VP15 of white spot syndrome virus (WSSV) and glycosylation status of the WSSV major structural proteins.

نویسندگان

  • Mariëlle C W van Hulten
  • Martin Reijns
  • Angela M G Vermeesch
  • Fokko Zandbergen
  • Just M Vlak
چکیده

White spot syndrome virus (WSSV) infects penaeid shrimp and other crustaceans. The WSSV virion consists of an enveloped rod-shaped nucleocapsid enclosing a large circular double-stranded DNA genome of 293 kbp. The virion envelope contains two major proteins of 28 (VP28) and 19 kDa (VP19) and the nucleocapsid consists of three major proteins of 26 (VP26), 24 (VP24) and 15 kDa (VP15). Study on the morphogenesis of the WSSV particle requires the genomic identification and chemical characterization of these WSSV virion proteins. An internal amino acid sequence of envelope protein VP19 was obtained by amino acid sequencing and used to locate the VP19 open reading frame of this protein on the genome, as WSSV ORF182. VP19 contained two putative transmembrane domains, which may anchor this protein in the WSSV envelope. Similarly, the gene for VP15 was located on the WSSV genome as ORF109. N-terminal amino acid sequencing on VP15 suggested that this protein was expressed from the second ATG of its ORF and the first methionine is lost by N-terminal protein processing. The 15 kDa protein is very basic and is a candidate DNA-binding protein in the WSSV nucleocapsid. None of the five major structural WSSV proteins appear to be glycosylated, which is an unusual feature among enveloped animal viruses.

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عنوان ژورنال:
  • The Journal of general virology

دوره 83 Pt 1  شماره 

صفحات  -

تاریخ انتشار 2002