English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Identification of structural protein relationships is likely to be important for virus assembly and anti-WSSV strategies. In this paper, VP90 of white spot syndrome virus (WSSV) was characterized. Temporal-transcription analysis showed that VP90 is expressed in the late stage of WSSV infection. Far-western and matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS) assay showed that VP90 interacts with VP26 and VP28, two major envelope proteins. Far-western blot with recombinant VP26 (rVP26), N-terminal end of VP28 (rVP28N) and C-terminal end of VP28 (rVP28C) provided further evidence for interaction of rVP90 and rVP26 or rVP28. These results suggest that VP90 is anchored to the envelope through interacting with VP26 and VP28.

VP90 of white spot syndrome virus interacts with VP26 and VP28