Characterization of iridovirus IV1 polypeptides: mapping by surface labelling

• Published in: Research in virology (Paris) 1997-05, Vol.148 (3), p.239-250
• Main Authors: Watson, D., Seligy, V.L.
• Format: Article
• Language: English
• Subjects: 2-D mapping; Animals; Biological and medical sciences; Capsid; Capsid - analysis; Capside; Cartographie 2-D; Chloramines - chemistry; Diptera - virology; Disulfides; Disulphide bonds; Electrophoresis, Gel, Two-Dimensional; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Iodine Radioisotopes; Iridovirus; Iridovirus - chemistry; Isotope Labeling; Lactoperoxidase - chemistry; Liaisons disulfures; Major structural protein; Microbiology; Morphology, structure, chemical composition, physicochemical properties; Peptide Mapping; Peptides - analysis; Polypeptide; Proteine de structure majeure; Sodium Dodecyl Sulfate; Tosyl Compounds - chemistry; Viral Envelope Proteins - analysis; Virology
• ISSN: 0923-2516
• DOI: 10.1016/S0923-2516(97)83994-5

A comprehensive index of IV1(Tipula iridescent virus, or TIV)-associated polypeptides has been established using enrichments of “empty” and “filled” virions that are considered to be maturation-phase-related. The mapping strategy which involved oneand two-dimensional polyacrylamide gel electrophoresis, silver staining, disulphide bond reduction and 125I iodination of putative surface proteins revealed 103 and 116 polypeptides for empty and filled capsids, respectively. These estimates could be reduced to ≤70 by reclassing multicharged polypeptides of approximately identical masses as single entities. At least 10 polypeptides from empty and filled virions were involved in intermolecular sulphhydryl linkages and another 11 species were identified as putative outer shell (surface) polypeptides. These data provide useful criteria for iridovirus classification and identification of candidate polypeptides involved in capsid formation and maturation. Les techniques utilisées (dont la ≪PAGE 2-D≫) ont permis de déceler respectivement 103 et 106 polypeptides à partir de virus ≪vides≫ et ≪pleins≫; mais seulement 10 polypeptides au total se montrent impliqués dans les liaisons disulfures. L'ensemble des données constitue un critère très utile pour la classification des iridovirus et pour l'identification des polypeptides impliqués dans la formation des capsides et la maturation.