Studies on the Structure of the Two Infectious Types of Densonucleosis Virus

Abstract

No electrophoretic differences were detected between the nucleic acids of the two types of densonucleosis virus, DNV-I and DNV-II. Both virus types had similar isoelectric points. Although the viral proteins found in each type were identical, their stoichiometry differed. The localization of the structural protein, by labeling with periodate-oxidized glycoprotein, supported the hypothesis that 60 molecules of p49 aggregated into a dodecahedron (12 pentamers), whereas the two other proteins (p59 and p69) might have a stabilizing function and were localized on the outer surface of the p49 dodecahedron.

Purification and characterization of the infectious hypodermal and haematopoietic necrosis virus of penaeid shrimps

“…The picornavirus polypeptides have MrS ranging from 35K to 6.5K, which are usually less than the smallest of the IHHNV polypeptides; the exception to this is the VP0 polypeptide (36.5K to 41K) which is found as a trace of a fifth chain in picornaviruses such as poliovirus, encephalomyocarditis virus, foot-and-mouth disease virus, human rhinovirus type 14 and murine encephalomyelitis virus (Rueckert, 1976(Rueckert, , 1986. On the other hand, the presence of four polypeptides in IHHNV could be related to similar findings in insect parvoviruses (densovirus; DNV) such as DNV from Galleria mellonella (Tijssen & Kurstak, 1979) and Pseudoplusia includens picarnavirus (Chao et al, 1985) or in a parvo-like virus (PC84) of crustacea (Mari & Bonami, 1988b).…”

The photochemical reaction center of Chloroflexus aurantiacus is composed of two structurally similar polypeptides

“…Peptide fragments produced by proteolysis or chemical cleavage were resolved on gradient polyacrylamide gels [27]. Electroblotting of NaDodS04 gels and detection of reaction center polypeptides and peptide fragments using anti-(reaction center) rabbit serum and horseradish-peroxidase-conjugated anti-(rabbit Ig) goat serum was done as described by Shiozawa et al [28].…”

The structure of an insect parvovirus (Galleria mellonella densovirus) at 3.7 å resolution

“…The 1.40 g/cm 3 form is stable in the presence of divalent cations, but removal of these cations induces a change in density to 1.44 g/cm 3 . Presumably, a conformational change accompanies the binding of divalent ions, although the two denser types of capsid appear to have similar morphologies when negatively stained virions are viewed with an electron microscope [16]. The change in virus density, mediated by the presence or absence of calcium and magnesium ions, implies that the virions have a specific divalent-cation-binding site.…”