Abstract:
:The budded phenotype of Autograha californica nuclear polyhedrosis virus (AcNPV BV) has a 64K glycoprotein in its envelope which is important in the ability of the virus to functionally enter host cells. Tunicamycin (TM), an inhibitor of N-linked glycosylation, was used to determine whether the sugar moiety was essential for the normal function of the 64K protein. At 10 mug/ml TM, glycosylation was completely inhibited. Infectivity of AcNPV BV was reduced to 2% of control while extracellular particles formed were 28% of control. Particles produced in the presence of 10 mug/ml TM were neutralizable by a monoclonal antibody reactive with the 64K envelope protein and their infectivity was sensitive to chloroquine. These results indicated that the major envelope protein, though unglycosylated, was still able to function normally in viral entry. Particles grown in the presence of 10 mug/ml TM however, contained on average, only 30% of the normal concentration of this major envelope protein. The combination of reduced number of extracellular particles and reduced amount of major envelope protein on these particles could account for the observed reduction in infectivity.
journal_name
Virologyjournal_title
Virologyauthors
Charlton CA,Volkman LEdoi
10.1016/0042-6822(86)90443-5subject
Has Abstractpub_date
1986-10-15 00:00:00pages
214-8issue
1eissn
0042-6822issn
1096-0341pii
0042-6822(86)90443-5journal_volume
154pub_type
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