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Fusion of a sendai mutant deficient in HN protein (ts271) with cardiolipin liposomes

Authors
Journal
Virology
0042-6822
Publisher
Elsevier
Publication Date
Volume
163
Issue
1
Identifiers
DOI: 10.1016/0042-6822(88)90254-1
Disciplines
  • Biology
  • Chemistry

Abstract

Abstract Sendai mutant ts271 contains <5% of the amount of HN glycoprotein found in wild-type Sendai. Fusion of this mutant with cardiolipin liposomes revealed no differences from the wild-type virus with regard to specific activity, pH dependence, or radiation inactivation. Target sizes of both mutant and wild-type viral proteins were determined by the radiation-induced disappearance of each band from an SDS-polyacrylamide gel and no differences were found. Of the viral proteins, only F had a target size corresponding to the monomer molecular weight, ca. 60 kDa, identical to the minimum unit previously determined by functional assay for Sendai virus-erythrocyte membrane fusion ( K. Bundo-Morita, S. Gibson, and J. Lenard, Biochemistry 26, 6223–6227 (1987) ). This provides additional evidence that F alone is the active protein mediating Sendai-erythrocyte fusion. It is concluded that the HN protein is unlikely to mediate any fusion reactions of the intact virions, either with biological membranes or with cardiolipin liposomes.

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