Abstract

The baculoviruses of marine penaeid shrimp, PmSNPV and PvSNPV (MBV type and BP type, respectively), have distinctly different occlusion bodies (OBs) from those of the insect baculoviruses. In contrast to insect baculovirus, the penaeid baculovirus OB is unenveloped and formed by large subunits (SuOBs), as observed by electron microscopy after negative staining. The polyhedrin subunits measure 17 to 23 nm in diameter and appear icosahedral, resembling full and empty viral particles. Although these SuOBs look similar in morphometrics to shrimp parvoviruses, their density, polypeptide composition, and UV spectra are more characteristic of proteins than nucleoproteins. Common to the two shrimp baculovirus OBs that were investigated is the aggregation of three icosahedral SuOBs into a triplet. The observed difference in their crystalline structure is directly related to the way in which triplets attach to each other to form the OB. In the BP-type OB, the triplets form alternating parallel rows in all three dimensions. On the other hand, in the MBV-type OB, four triplets form a hollow sphere which we call a “rosette,” the building blocks of the MBV-type OB. We assembled models for the penaeid baculovirus OB as an alternative to those hypothesized for insect baculovirus OBs.

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