Protein composition of the occlusion bodies of Epinotia aporema granulovirus

AbstractWithin family Baculoviridae, members of the Betabaculovirus genus are employed as biocontrol agents against lepidopteran pests, either alone or in combination with selected members of the Alphabaculovirus genus. Epinotia aporema granulovirus (EpapGV) is a fast killing betabaculovirus that infects the bean shoot borer (E. aporema) and is a promising biopesticide. Because occlusion bodies (OBs) play a key role in baculovirus horizontal transmission, we investigated the composition of EpapGV OBs. Using mass spectrometry-based proteomics we could identify 56 proteins that are included in the OBs during the final stages of larval infection. Our data provides experimental validation of several annotated hypothetical coding sequences. Proteogenomic mapping against genomic sequence detected a previously unannotated ac110-like core gene and a putative translation fusion product of ORFs epap48 and epap49. Comparative studies of the proteomes available for the family Baculoviridae highlight the conservation of core gene products as parts of the occluded virion. Two proteins specific for betabaculoviruses (Epap48 and Epap95) are incorporated into OBs. Moreover, quantification based on emPAI values showed that Epap95 is one of the most abundant components of EpapGV OBs.

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Characterization of a Granulovirus Isolated from Epinotia aporema Wals. (Lepidoptera: Tortricidae) Larvae

Applied and Environmental Microbiology ◽

10.1128/aem.67.8.3702-3706.2001 ◽

2001 ◽

Vol 67 (8) ◽

pp. 3702-3706 ◽

Cited By ~ 19

Author(s):

Alicia Sciocco-Cap ◽

Alejandro D. Parola ◽

Alina V. Goldberg ◽

Pablo D. Ghiringhelli ◽

Vı́ctor Romanowski

Keyword(s):

Biological Control ◽

High Specificity ◽

Biological Properties ◽

Terminal Sequence ◽

Amino Terminal ◽

Soybean Pest ◽

Occlusion Bodies ◽

Amino Terminal Sequence ◽

Epinotia Aporema

ABSTRACT A granulovirus (GV) isolated from Epinotia aporema(Lepidoptera: Tortricidae)—a major soybean pest—was studied in terms of its main morphological, biochemical, and biological properties. The ovoidal occlusion bodies were 466 by 296 nm in size, and their most prominent protein had an apparent molecular mass of 29 kDa. Its amino-terminal sequence was remarkably homologous to that of the granulins of other GVs. The DNA genome size was estimated to be 120 kbp. The high specificity and pathogenicity of this newly described granulovirus (EpapGV) indicate that it is indeed a good candidate for the biological control of this pest.

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Light microscopy of microsporidian spores and baculovirus occlusion bodies in Epinotia aporema and Helicoverpa gelotopoeon larval tissues, respectively

Revista Argentina de Microbiología ◽

10.1016/j.ram.2016.04.008 ◽

2016 ◽

Vol 48 (4) ◽

pp. 358-359

Author(s):

Joel D. Arneodo ◽

Catalina Taibo ◽

Alicia Sciocco-Cap

Keyword(s):

Light Microscopy ◽

Occlusion Bodies ◽

Epinotia Aporema

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Bovine Platelet Proteins

Thrombosis and Haemostasis ◽

10.1055/s-0038-1653555 ◽

1969 ◽

Vol 21 (03) ◽

pp. 409-418 ◽

Cited By ~ 2

Author(s):

S Łopaciuk ◽

N. O Solum

Keyword(s):

Bovine Serum ◽

Protein Composition ◽

Disc Electrophoresis ◽

Plasma Fibrinogen ◽

Plasma Albumin ◽

Precipitin Line ◽

Bovine Plasma ◽

Platelet Proteins

Summary1. The protein composition of bovine platelet extracts has been investigated by immunoelectrophoresis and polyacrylamide disc electrophoresis. The information obtained is discussed as a basis for study on platelet fibrinogen.2. With antiserum to platelet proteins 11 precipitin lines were observed 3 of which corresponded electrophoretically to plasma albumin, fibrinogen and γ-globulin. These lines were not seen using the same antiserum absorbed with bovine plasma. The 8 additional lines were still present indicating that they represented specific platelet components. Antiserum to plasma produced the 3 above-mentioned lines, but no others.3. With antiserum to purified bovine plasma fibrinogen 3 precipitin lines were observed. The fibrinogen line was the dominant one. The 2 additional lines did not disappear by absorption of the antiserum with bovine serum nor by incubation of the extracts with thrombin. The latter treatment totally removed the fibrinogen line.4. A non-fibrinogen precipitin line, observed only with the antiserum to platelet extract and positioned in the β2-globulin region, disappeared by the incubation of platelet extracts with thrombin.

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