Resistance of the 64K protein of budded Autographa californica nuclear polyhedrosis virus to functional inactivation by proteolysis.

Abstract:

:The 64K surface protein of budded Autographa californica nuclear polyhedrosis virus (AcMNPV BV) is known to play a role in the functional entry of AcMNPV BV into Spodoptera frugiperda IPLB-SF-21 cells by adsorptive endocytosis. AcV1, a neutralizing monoclonal antibody, reacts with the 64K protein and in doing so prevents efficient entry. In this communication we report that treatment of AcMNPV BV with either trypsin or proteinase K cleaves the 64K protein into one major fragment of 34.6K and two minor fragments of 36K to 37.2K that are retained with the virus. All of the fragments are glycosylated. Protease treatment does not reduce viral infectivity, but it does result in the destruction of the AcV1-reactive epitope; thus AcV1 is not able to neutralize protease-treated AcMNPV BV. Polyclonal antiserum to BV is able to recognize both cleaved and uncleaved 64K and neutralize both protease-treated and untreated virus. Protease treatment does not diminish the sensitivity of AcMNPV BV to chloroquine, but it does cause the virus to become more susceptible to inactivation by 2-mercaptoethanol (2-ME) even though exposure to 2-ME does not result in dissociation of the fragments from the virus.

journal_name

Virology

journal_title

Virology

authors

Volkman LE,Goldsmith PA

doi

10.1016/0042-6822(88)90176-6

subject

Has Abstract

pub_date

1988-09-01 00:00:00

pages

285-9

issue

1

eissn

0042-6822

issn

1096-0341

journal_volume

166

pub_type

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