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Structure of Penaeus stylirostris densovirus, a shrimp pathogen
Bärbel Kaufmann1, Valorie D Bowman, Yi Li
1Department of Biological Sciences, Purdue University, 915 West State Street, West Lafayette, IN 47907-2054, USA.
Journal of Virology
|August 13, 2010
Summary
Penaeus stylirostris densovirus (PstDNV) has a unique, small capsid protein structure. This structural analysis provides insights into Brevidensovirus genus and PstDNV infection mechanisms.
Area of Science:
- Virology
- Structural Biology
- Aquaculture Pathology
Background:
- Penaeus stylirostris densovirus (PstDNV) is a significant pathogen affecting penaeid shrimp.
- Unlike other parvoviruses, PstDNV lacks phospholipase A2 activity, crucial for host cell infection.
Purpose of the Study:
- To determine the near-atomic resolution structure of PstDNV virus-like particles.
- To understand the structural basis of PstDNV capsid protein and its implications for viral infection.
Main Methods:
- X-ray crystallography was used to determine the structure of recombinant PstDNV virus-like particles.
- The structure was resolved to 2.5-Å resolution.
Main Results:
- The PstDNV capsid is composed of 60 copies of a 37.5-kDa coat protein, the smallest reported for parvoviruses.
- The capsid protein exhibits a β-barrel 'jelly roll' motif, common in icosahedral viruses.
- A unique 'domain-swapped' conformation was observed in the N-terminal portion, differing from vertebrate parvoviruses but similar to insect parvoviruses.
Conclusions:
- This is the first near-atomic resolution structure for the Brevidensovirus genus.
- The distinct structural features of the PstDNV capsid protein may influence its host cell interactions and pathogenesis.
- Further research can leverage this structural information to develop antiviral strategies for shrimp aquaculture.
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