Fatty acid acylation of the 67K envelope glycoprotein of a baculovirus: Autographa californica nuclear polyhedrosis virus.
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]palmitic acid and [3H]myristic acid-labeled gp67. Acyl peptides were protected during proteinase K digestion of intact virions but they were larger (Mr 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.
Roberts
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Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, Canada.
Faulkner
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P
D000215:Acylation; D000595:Amino Acid Sequence; D007304:Insect Viruses / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000235:genetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D014759:Viral Envelope Proteins / Q000378:metabolism*
D008562:Membrane Glycoproteins; D010750:Phosphoproteins; D014759:Viral Envelope Proteins