Abstract
Modification of Autographa californica multicapsid nuclear polyhedrosis virus extracellular virion polypeptides with fatty acid was investigated. Fatty acid-derived radioactivity was incorporated into gp67, the predominant virion envelope glycoprotein, during metabolic labeling using [ 3H]palmitic acid or [ 3H]myristic acid. The acyl moiety resisted extraction with chloroform-methanol but was released by mild alkali or hydroxylamine treatment, features characteristic of an ester-type linkage. Palmitic acid was identified as the fatty acid liberated during acid hydrolysis of purified [ 3H]pal-mitic acid and [ 3H]myristic acid-labeled gp67. Acyl peptides were protected during proteinase K digestion of intact virions but they were larger ( M r , 34.3K and 31.8K) than expected on the basis of membrane protection alone. Carbohydrate may have played a role in determining the protease resistance of the observed fragments. Potential acylation sites on gp67 within or adjacent to the C-terminal hydrophobic region are discussed with respect to the predicted amino acid sequence.
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