scholarly journals The complete amino acid sequence of Selenephera lunigera nuclear polyhedrosis virus polyhedrin

2002 ◽  
Vol 18 (4) ◽  
pp. 279-282
Author(s):  
E. A. Kozlov ◽  
T. L. Levitina ◽  
M. T. Bobrovskaja ◽  
M. N. Ovander
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Nuclear Polyhedrosis Virus ◽  
Complete Amino Acid Sequence ◽  
Polyhedrosis Virus ◽  
Nuclear Polyhedrosis

scholarly journals Effects of Substituting Granulin or a Granulin-Polyhedrin Chimera for Polyhedrin on Virion Occlusion and Polyhedral Morphology in Autographa californicaMultinucleocapsid Nuclear Polyhedrosis Virus

1998 ◽  
Vol 72 (7) ◽  
pp. 6237-6243 ◽  
Author(s):  
Jane E. Eason ◽  
Robert H. Hice ◽  
Jeffrey J. Johnson ◽  
Brian A. Federici
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Trichoplusia Ni ◽  
Nuclear Polyhedrosis Virus ◽  
Occlusion Body ◽  
Wild Type ◽  
Unusual Structure ◽  
Primary Amino ◽  
Polyhedrosis Virus ◽  
Nuclear Polyhedrosis

ABSTRACT Substitution of granulin from the Trichoplusia nigranulosis virus (TnGV) for polyhedrin of the Autographa californica multinucleocapsid nuclear polyhedrosis virus (AcMNPV) yielded a few very large (2 to 5 μm) cuboidal inclusions in the cytoplasm and nucleus of infected cells. These polyhedra lacked the beveled edges characteristic of wild-type AcMNPV polyhedra, contained fractures, and occluded few virions. Placing a nuclear localization signal (KRKK) in granulin directed more granulin to the nucleus and resulted in more structurally uniform cuboidal inclusions in which no virions were observed. A granulin-polyhedrin chimera produced tetrahedral occlusions with more virions than granulin inclusions but many fewer than wild-type polyhedra. Despite the unusual structure of the granulin and granulin-polyhedrin inclusions, they interacted with AcMNPV p10 fibrillar structures and electron-dense spacers that are precursors of the polyhedral calyx. The change in inclusion shape obtained with the granulin-polyhedrin chimera demonstrates that the primary amino acid sequence affects occlusion body shape, but the large cuboidal inclusions formed by granulin indicate that the amino acid sequence is not the only determinant. The failure of granulin or the granulin-polyhedrin chimera to properly occlude AcMNPV virions suggests that specific interactions occur between polyhedrin and other viral proteins which facilitate normal virion occlusion and occlusion body assembly and shape in baculoviruses.

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence
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