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ENTOMOPOXVIRUSES ASSOCIATED WITH GRASSHOPPERS AND LOCUSTS: BIOCHEMICAL CHARACTERIZATION

Published online by Cambridge University Press:  31 May 2012

M.A. Erlandson  and
D.A. Streett
M.A. Erlandson
Affiliation:
Agriculture and Agri-Food Canada Research Centre, 107 Science Place, Saskatoon, Saskatchewan, Canada S7N 0X2
D.A. Streett
Affiliation:
USDA/ARS, Rangeland Insect Laboratory, Montana State University, Bozeman, Montana, USA 59717-0366
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Abstract

Entomopoxviruses (EPVs) are large DNA viruses with structural similarities to vertebrate poxviruses. EPV virions are occluded in large (3–15 μm in diameter) proteinaceous occlusion bodies (OBs). To date, EPVs are reported from 15 species of grasshoppers and locusts. The current information on the biochemical characterization of these EPVs is summarized in our review. The DNA genomes of grasshopper and locust EPVs analysed to date have a G+C ratio of approximately 18.5% and genome size estimates generated by various methods range from 180 to 194 kilobase pairs (kbp). Restriction endonuclease enzyme analysis of a number of grasshopper and locust EPV DNAs shows the virus isolates to be distinct and the technique will be useful in identifying virus isolates. The structural proteins of certain grasshopper EPVs have also been analysed. Forty to 50 polypeptides ranging in molecular weight from 12 to 200 kilodaltons (kDa) have been detected by SDS-PAGE analysis of virions released from OBs and the polypeptide profiles are distinct for many of the virus isolates. The proteinaceous matrix of the OB of EPVs contains one predominant protein referred to as spheroidin. The spheroidin protein from most grasshopper EPVs is approximately the same molecular weight, 107 kDa, when analysed by SDS-PAGE. As with other groups of occluded insect viruses, grasshopper EPVs have a protease activity associated with OBs derived from infected insects. The possible role of this protease activity in the infection cycle is discussed. Finally, the role of various molecular techniques for the detection and identification of EPV infections in laboratory and field populations of grasshoppers and locusts is discussed. The development of EPV-specific monoclonal antibodies and DNA hybridization probes for the detection of virus infections is reviewed. As well, the possible use of polymerase chain reaction and randomly amplified polymorphic DNA fingerprinting techniques for the detection and identification of EPV infections is discussed.

Résumé

Les entomopoxvirus (EPV) sont des virus d'ADN dont la structure ressemble à celle des poxvirus de vertébrés. Les virions des EPV sont enfermés dans des corps d'inclusion protéinés de grande taille (3–15 μm de diamètre). à ce jour, des EPV ont été signalés chez 15 espèces de criquets. Les informations actuelles sur les propriétés biochimiques de ces EPV sont résumées. Les génomes d'ADN des EPV de criquets connus ont un rapport G+C d'environ 18,5% et la taille théorique de génomes, estimée par différente méthodes, va de 180 à 194 paires de kilobases (kbp). L'analyse des fragments polymorphiques d'ADN des EPV de plusieurs criquets au moyen d'endonucléases de restriction a démontré que les isolats des virus sont distincts et que la technique s'avérera très utile dans l'identification des isolats de virus. Les protéines structurelles de certains EPV de criquets ont également été analysées. De 40 à 50 polypeptides de masse moléculaire allant de 12 à 20 kilodaltons (kDa) ont été reconnus par analyse de protéines par gel d'électrophorèse (SDS-PAGE) des virions libérés des corps d'inclusion et les profils de ces polypeptides sont spécifiques dans le cas de plusieurs des isolats de virus. La matrice protéinique des corps d'inclusion des EPV contient une protéine prédominante appelée ici sphéroïdine. La sphéroïdine de la plupart des EPV de criquets a à peu près toujours la même masse moléculaire, soit 107 kDa selon une analyse SDS-PAGE. Comme la plupart des autres groupes de virus d'insectes contenus dans des corps d'inclusion, les EPV de criquets possèdent une protéase associée aux corps d'inclusion qui leur vient des insectes infectés. Le rôle possible de l'activité de la protéase dans le cycle de l'infection fait l'objet d'une discussion. Enfin, l'efficacité de diverses techniques moléculaires dans le dépistage et l'identification des infections d'entomopoxvirus au sein des populations expérimentales et naturelles de criquets est examinée. Nous examinons où en est le progrès dans l'élaboration d'anticorps monoclonaux spécifiques aux EPV et de sondes d'hybridation de l'ADN pour le dépistage des infections virales. De même, la possibilité d'utiliser la polymérisation par réaction en chaîne et les techniques d'amplification aléatoire de l'ADN polymorphe pour dépister et identifier les infections par des EPV est examinée également. [Traduit par la Rédaction]

Type
Research Article
Information
The Memoirs of the Entomological Society of Canada , Volume 129 , Supplement S171 , 1997 , pp. 131 - 146
Copyright
Copyright © Entomological Society of Canada 1997

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Footnotes

1

Contribution No. 1154 from the Saskatchewan Research Centre.

2

Present address: USDA/ARS, Southern Insect Management Unit, P.O. Box 346, Stoneville, Mississippi. 38776 U.S.A.

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